Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.
Identifieur interne : 000F60 ( Main/Corpus ); précédent : 000F59; suivant : 000F61Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.
Auteurs : Kamel Chibani ; Frederick Saul ; Claude Didierjean ; Nicolas Rouhier ; Ahmed HaouzSource :
- FEBS letters [ 1873-3468 ] ; 2018.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Chloroplast Proteins, Thioredoxins.
- chemical , genetics : Chloroplast Proteins, Thioredoxins.
- enzymology : Populus.
- genetics : Populus.
- Catalysis, Catalytic Domain, Crystallography, X-Ray, Mutation, Oxidation-Reduction.
Abstract
Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modeling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases (FTR) indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial FTR.
DOI: 10.1002/1873-3468.13009
PubMed: 29453875
Links to Exploration step
pubmed:29453875Le document en format XML
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CRM2, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation><nlm:affiliation>UMR 1136, Interactions Arbres-Microorganismes, Faculté des Sciences et Technologies, Université de Lorraine/INRA, Vandœuvre-lès-Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name><affiliation><nlm:affiliation>Institut Pasteur, Plateforme de Cristallographie, CNRS-UMR 3528, Paris, France.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29453875</idno><idno type="pmid">29453875</idno><idno type="doi">10.1002/1873-3468.13009</idno><idno type="wicri:Area/Main/Corpus">000F60</idno><idno type="wicri:explorRef" wicri:stream="Main" 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Didierjean</name><affiliation><nlm:affiliation>Université de Lorraine, CNRS, CRM2, Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation><nlm:affiliation>UMR 1136, Interactions Arbres-Microorganismes, Faculté des Sciences et Technologies, Université de Lorraine/INRA, Vandœuvre-lès-Nancy, France.</nlm:affiliation></affiliation></author><author><name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name><affiliation><nlm:affiliation>Institut Pasteur, Plateforme de Cristallographie, CNRS-UMR 3528, Paris, France.</nlm:affiliation></affiliation></author></analytic><series><title level="j">FEBS letters</title><idno type="eISSN">1873-3468</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalysis (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Chloroplast Proteins (chemistry)</term><term>Chloroplast Proteins (genetics)</term><term>Crystallography, X-Ray (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chloroplast Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Chloroplast Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Catalytic Domain</term><term>Crystallography, X-Ray</term><term>Mutation</term><term>Oxidation-Reduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modeling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases (FTR) indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial FTR.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29453875</PMID><DateCompleted><Year>2019</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN><JournalIssue CitedMedium="Internet"><Volume>592</Volume><Issue>6</Issue><PubDate><Year>2018</Year><Month>03</Month></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.</ArticleTitle><Pagination><MedlinePgn>1030-1041</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/1873-3468.13009</ELocationID><Abstract><AbstractText>Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modeling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases (FTR) indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial FTR.</AbstractText><CopyrightInformation>© 2018 Federation of European Biochemical Societies.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chibani</LastName><ForeName>Kamel</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>UMR 1136, Interactions Arbres-Microorganismes, Faculté des Sciences et Technologies, Université de Lorraine/INRA, Vandœuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Saul</LastName><ForeName>Frederick</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Plateforme de Cristallographie, CNRS-UMR 3528, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Université de Lorraine, CNRS, CRM2, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>UMR 1136, Interactions Arbres-Microorganismes, Faculté des Sciences et Technologies, Université de Lorraine/INRA, Vandœuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haouz</LastName><ForeName>Ahmed</ForeName><Initials>A</Initials><Identifier Source="ORCID">0000-0003-1196-1635</Identifier><AffiliationInfo><Affiliation>Institut Pasteur, Plateforme de Cristallographie, CNRS-UMR 3528, Paris, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016422">Letter</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>03</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D060365">Chloroplast Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D060365" MajorTopicYN="N">Chloroplast Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="Y">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Populus
</Keyword><Keyword MajorTopicYN="Y">atypical thioredoxin</Keyword><Keyword MajorTopicYN="Y">crystal structure</Keyword><Keyword MajorTopicYN="Y">disulfide exchange</Keyword><Keyword MajorTopicYN="Y">glutathione</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>12</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>01</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>02</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29453875</ArticleId><ArticleId IdType="doi">10.1002/1873-3468.13009</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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