Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle.
Identifieur interne : 000207 ( Main/Exploration ); précédent : 000206; suivant : 000208Arabidopsis and Chlamydomonas phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle.
Auteurs : Libero Gurrieri [Italie] ; Alessandra Del Giudice [Italie] ; Nicola Demitri [Italie] ; Giuseppe Falini [Italie] ; Nicolae Viorel Pavel [Italie] ; Mirko Zaffagnini [Italie] ; Maurizio Polentarutti [Italie] ; Pierre Crozet [France] ; Christophe H. Marchand [France] ; Julien Henri [France] ; Paolo Trost [Italie] ; Stéphane D. Lemaire [France] ; Francesca Sparla [Italie] ; Simona Fermani [Italie]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2019.
Descripteurs français
- KwdFr :
- Arabidopsis (composition chimique), Arabidopsis (enzymologie), Chlamydomonas (composition chimique), Chlamydomonas (enzymologie), Cristallographie (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Phosphotransferases (Alcohol Group Acceptor) (composition chimique), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Photosynthèse (physiologie), Protéines végétales (composition chimique), Protéines végétales (métabolisme), Protéome (composition chimique).
- MESH :
- composition chimique : Arabidopsis, Chlamydomonas, Phosphotransferases (Alcohol Group Acceptor), Protéines végétales, Protéome.
- enzymologie : Arabidopsis, Chlamydomonas.
- métabolisme : Phosphotransferases (Alcohol Group Acceptor), Protéines végétales.
- physiologie : Photosynthèse.
- Cristallographie, Modèles moléculaires, Oxydoréduction.
English descriptors
- KwdEn :
- Arabidopsis (chemistry), Arabidopsis (enzymology), Chlamydomonas (chemistry), Chlamydomonas (enzymology), Crystallography (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Phosphotransferases (Alcohol Group Acceptor) (chemistry), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Photosynthesis (physiology), Plant Proteins (chemistry), Plant Proteins (metabolism), Proteome (chemistry).
- MESH :
- chemical , chemistry : Phosphotransferases (Alcohol Group Acceptor), Plant Proteins, Proteome.
- chemistry : Arabidopsis, Chlamydomonas.
- enzymology : Arabidopsis, Chlamydomonas.
- chemical , metabolism : Phosphotransferases (Alcohol Group Acceptor), Plant Proteins.
- physiology : Photosynthesis.
- Crystallography, Models, Molecular, Oxidation-Reduction.
Abstract
In land plants and algae, the Calvin-Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga Chlamydomonas reinhardtii (CrPRK) and the land plant Arabidopsis thaliana (AtPRK). PRK is an elongated homodimer characterized by a large central β-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 Å apart and connected by a flexible region exclusive to photosynthetic eukaryotes-the clamp loop-which is believed to be essential for oxidation-induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both AtPRK and CrPRK have a strongly reduced dimer interface and an increased number of random-coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes.
DOI: 10.1073/pnas.1820639116
PubMed: 30923119
PubMed Central: PMC6475412
Affiliations:
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Ciamician, University of Bologna, 40126 Bologna, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry G. 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Marchand</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Henri, Julien" sort="Henri, Julien" uniqKey="Henri J" first="Julien" last="Henri">Julien Henri</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Trost, Paolo" sort="Trost, Paolo" uniqKey="Trost P" first="Paolo" last="Trost">Paolo Trost</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="Lemaire, Stephane D" sort="Lemaire, Stephane D" uniqKey="Lemaire S" first="Stéphane D" last="Lemaire">Stéphane D. Lemaire</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Sparla, Francesca" sort="Sparla, Francesca" uniqKey="Sparla F" first="Francesca" last="Sparla">Francesca Sparla</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy; francesca.sparla@unibo.it simona.fermani@unibo.it.</nlm:affiliation><country wicri:rule="url">Italie</country><wicri:regionArea>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="Fermani, Simona" sort="Fermani, Simona" uniqKey="Fermani S" first="Simona" last="Fermani">Simona Fermani</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy; francesca.sparla@unibo.it simona.fermani@unibo.it.</nlm:affiliation><country wicri:rule="url">Italie</country><wicri:regionArea>Department of Chemistry G. 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Ciamician, University of Bologna, 40126 Bologna, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry G. Ciamician, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="Pavel, Nicolae Viorel" sort="Pavel, Nicolae Viorel" uniqKey="Pavel N" first="Nicolae Viorel" last="Pavel">Nicolae Viorel Pavel</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Rome Sapienza, 00185 Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Chemistry, University of Rome Sapienza, 00185 Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="Polentarutti, Maurizio" sort="Polentarutti, Maurizio" uniqKey="Polentarutti M" first="Maurizio" last="Polentarutti">Maurizio Polentarutti</name><affiliation wicri:level="1"><nlm:affiliation>Elettra-Sincrotrone Trieste, 34149 Basovizza, Trieste, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Elettra-Sincrotrone Trieste, 34149 Basovizza, Trieste</wicri:regionArea><wicri:noRegion>Trieste</wicri:noRegion></affiliation></author><author><name sortKey="Crozet, Pierre" sort="Crozet, Pierre" uniqKey="Crozet P" first="Pierre" last="Crozet">Pierre Crozet</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Marchand, Christophe H" sort="Marchand, Christophe H" uniqKey="Marchand C" first="Christophe H" last="Marchand">Christophe H. Marchand</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Henri, Julien" sort="Henri, Julien" uniqKey="Henri J" first="Julien" last="Henri">Julien Henri</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Trost, Paolo" sort="Trost, Paolo" uniqKey="Trost P" first="Paolo" last="Trost">Paolo Trost</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="Lemaire, Stephane D" sort="Lemaire, Stephane D" uniqKey="Lemaire S" first="Stéphane D" last="Lemaire">Stéphane D. Lemaire</name><affiliation wicri:level="3"><nlm:affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Sparla, Francesca" sort="Sparla, Francesca" uniqKey="Sparla F" first="Francesca" last="Sparla">Francesca Sparla</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy; francesca.sparla@unibo.it simona.fermani@unibo.it.</nlm:affiliation><country wicri:rule="url">Italie</country><wicri:regionArea>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author><author><name sortKey="Fermani, Simona" sort="Fermani, Simona" uniqKey="Fermani S" first="Simona" last="Fermani">Simona Fermani</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy; francesca.sparla@unibo.it simona.fermani@unibo.it.</nlm:affiliation><country wicri:rule="url">Italie</country><wicri:regionArea>Department of Chemistry G. Ciamician, University of Bologna, 40126 Bologna</wicri:regionArea><wicri:noRegion>40126 Bologna</wicri:noRegion></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (chemistry)</term><term>Arabidopsis (enzymology)</term><term>Chlamydomonas (chemistry)</term><term>Chlamydomonas (enzymology)</term><term>Crystallography (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (chemistry)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Photosynthesis (physiology)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (metabolism)</term><term>Proteome (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (composition chimique)</term><term>Arabidopsis (enzymologie)</term><term>Chlamydomonas (composition chimique)</term><term>Chlamydomonas (enzymologie)</term><term>Cristallographie (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (composition chimique)</term><term>Phosphotransferases (Alcohol Group Acceptor) (métabolisme)</term><term>Photosynthèse (physiologie)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (métabolisme)</term><term>Protéome (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Plant Proteins</term><term>Proteome</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Arabidopsis</term><term>Chlamydomonas</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Arabidopsis</term><term>Chlamydomonas</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines végétales</term><term>Protéome</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term><term>Chlamydomonas</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term><term>Chlamydomonas</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Photosynthèse</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Photosynthesis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography</term><term>Models, Molecular</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallographie</term><term>Modèles moléculaires</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In land plants and algae, the Calvin-Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga <i>Chlamydomonas reinhardtii</i> (<i>Cr</i>PRK) and the land plant <i>Arabidopsis thaliana</i> (<i>At</i>PRK). PRK is an elongated homodimer characterized by a large central β-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 Å apart and connected by a flexible region exclusive to photosynthetic eukaryotes-the clamp loop-which is believed to be essential for oxidation-induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both <i>At</i>PRK and <i>Cr</i>PRK have a strongly reduced dimer interface and an increased number of random-coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30923119</PMID><DateCompleted><Year>2020</Year><Month>03</Month><Day>23</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>116</Volume><Issue>16</Issue><PubDate><Year>2019</Year><Month>04</Month><Day>16</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle><i>Arabidopsis</i> and <i>Chlamydomonas</i> phosphoribulokinase crystal structures complete the redox structural proteome of the Calvin-Benson cycle.</ArticleTitle><Pagination><MedlinePgn>8048-8053</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1820639116</ELocationID><Abstract><AbstractText>In land plants and algae, the Calvin-Benson (CB) cycle takes place in the chloroplast, a specialized organelle in which photosynthesis occurs. Thioredoxins (TRXs) are small ubiquitous proteins, known to harmonize the two stages of photosynthesis through a thiol-based mechanism. Among the 11 enzymes of the CB cycle, the TRX target phosphoribulokinase (PRK) has yet to be characterized at the atomic scale. To accomplish this goal, we determined the crystal structures of PRK from two model species: the green alga <i>Chlamydomonas reinhardtii</i> (<i>Cr</i>PRK) and the land plant <i>Arabidopsis thaliana</i> (<i>At</i>PRK). PRK is an elongated homodimer characterized by a large central β-sheet of 18 strands, extending between two catalytic sites positioned at its edges. The electrostatic surface potential of the catalytic cavity has both a positive region suitable for binding the phosphate groups of substrates and an exposed negative region to attract positively charged TRX-f. In the catalytic cavity, the regulatory cysteines are 13 Å apart and connected by a flexible region exclusive to photosynthetic eukaryotes-the clamp loop-which is believed to be essential for oxidation-induced structural rearrangements. Structural comparisons with prokaryotic and evolutionarily older PRKs revealed that both <i>At</i>PRK and <i>Cr</i>PRK have a strongly reduced dimer interface and an increased number of random-coiled regions, suggesting that a general loss in structural rigidity correlates with gains in TRX sensitivity during the molecular evolution of PRKs in eukaryotes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gurrieri</LastName><ForeName>Libero</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Del Giudice</LastName><ForeName>Alessandra</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Rome Sapienza, 00185 Rome, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Demitri</LastName><ForeName>Nicola</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Elettra-Sincrotrone Trieste, 34149 Basovizza, Trieste, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Falini</LastName><ForeName>Giuseppe</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pavel</LastName><ForeName>Nicolae Viorel</ForeName><Initials>NV</Initials><AffiliationInfo><Affiliation>Department of Chemistry, University of Rome Sapienza, 00185 Rome, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zaffagnini</LastName><ForeName>Mirko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Polentarutti</LastName><ForeName>Maurizio</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Elettra-Sincrotrone Trieste, 34149 Basovizza, Trieste, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Crozet</LastName><ForeName>Pierre</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Marchand</LastName><ForeName>Christophe H</ForeName><Initials>CH</Initials><Identifier Source="ORCID">0000-0002-0729-3841</Identifier><AffiliationInfo><Affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Henri</LastName><ForeName>Julien</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Trost</LastName><ForeName>Paolo</ForeName><Initials>P</Initials><Identifier Source="ORCID">0000-0002-6347-8701</Identifier><AffiliationInfo><Affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lemaire</LastName><ForeName>Stéphane D</ForeName><Initials>SD</Initials><AffiliationInfo><Affiliation>Institut de Biologie Physico-Chimique, UMR8226, CNRS, Sorbonne Université, 75005 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sparla</LastName><ForeName>Francesca</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Pharmacy and Biotechnology-FaBiT, University of Bologna, 40126 Bologna, Italy; francesca.sparla@unibo.it simona.fermani@unibo.it.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fermani</LastName><ForeName>Simona</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0002-3056-3432</Identifier><AffiliationInfo><Affiliation>Department of Chemistry G. Ciamician, University of Bologna, 40126 Bologna, Italy; francesca.sparla@unibo.it simona.fermani@unibo.it.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>6H7G</AccessionNumber><AccessionNumber>6H7H</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>03</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.19</RegistryNumber><NameOfSubstance UI="C022390">phosphoribulokinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Proc Natl Acad Sci U S A. 2019 Nov 19;116(47):23862</RefSource><PMID Version="1">31712443</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="Y">Arabidopsis</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002696" MajorTopicYN="Y">Chlamydomonas</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003461" MajorTopicYN="N">Crystallography</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010788" MajorTopicYN="N">Photosynthesis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">3D structure</Keyword><Keyword MajorTopicYN="Y">Calvin–Benson cycle</Keyword><Keyword MajorTopicYN="Y">phosphoribulokinase</Keyword><Keyword MajorTopicYN="Y">redox regulation</Keyword><Keyword MajorTopicYN="Y">thioredoxin</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate 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first="Paolo" last="Trost">Paolo Trost</name><name sortKey="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name></country><country name="France"><region name="Île-de-France"><name sortKey="Crozet, Pierre" sort="Crozet, Pierre" uniqKey="Crozet P" first="Pierre" last="Crozet">Pierre Crozet</name></region><name sortKey="Henri, Julien" sort="Henri, Julien" uniqKey="Henri J" first="Julien" last="Henri">Julien Henri</name><name sortKey="Lemaire, Stephane D" sort="Lemaire, Stephane D" uniqKey="Lemaire S" first="Stéphane D" last="Lemaire">Stéphane D. 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