The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.
Identifieur interne : 000A71 ( Main/Exploration ); précédent : 000A70; suivant : 000A72The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.
Auteurs : Yvonne Carius [Allemagne] ; Dagmar Rother ; Cornelius G. Friedrich ; Axel J. ScheidigSource :
- Acta crystallographica. Section D, Biological crystallography [ 1399-0047 ] ; 2009.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Dimérisation (MeSH), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Modèles moléculaires (MeSH), Motifs d'acides aminés (MeSH), Oxidoreductases acting on sulfur group donors (métabolisme), Oxydoréduction (MeSH), Paracoccus pantotrophus (enzymologie), Protein-disulfide reductase (glutathione) (composition chimique), Protein-disulfide reductase (glutathione) (physiologie), Protéines bactériennes (composition chimique), Protéines bactériennes (métabolisme), Protéines bactériennes (physiologie), Protéines de fusion recombinantes (composition chimique), Relation structure-activité (MeSH), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Soufre (métabolisme), Sélénométhionine (composition chimique), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique).
- MESH :
- composition chimique : Glutarédoxines, Protein-disulfide reductase (glutathione), Protéines bactériennes, Protéines de fusion recombinantes, Sélénométhionine, Thiorédoxines.
- enzymologie : Paracoccus pantotrophus.
- métabolisme : Disulfures, Oxidoreductases acting on sulfur group donors, Protéines bactériennes, Soufre.
- physiologie : Protein-disulfide reductase (glutathione), Protéines bactériennes.
- Alignement de séquences, Conformation des protéines, Cristallographie aux rayons X, Dimérisation, Données de séquences moléculaires, Modèles moléculaires, Motifs d'acides aminés, Oxydoréduction, Relation structure-activité, Similitude de séquences d'acides aminés, Sites de fixation, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Bacterial Proteins (physiology), Binding Sites (MeSH), Crystallography, X-Ray (MeSH), Dimerization (MeSH), Disulfides (metabolism), Glutaredoxins (chemistry), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Paracoccus pantotrophus (enzymology), Protein Conformation (MeSH), Protein Disulfide Reductase (Glutathione) (chemistry), Protein Disulfide Reductase (Glutathione) (physiology), Recombinant Fusion Proteins (chemistry), Selenomethionine (chemistry), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Structure-Activity Relationship (MeSH), Sulfur (metabolism), Thioredoxins (chemistry).
- MESH :
- chemical , chemistry : Bacterial Proteins, Glutaredoxins, Protein Disulfide Reductase (Glutathione), Recombinant Fusion Proteins, Selenomethionine, Thioredoxins.
- chemical , metabolism : Bacterial Proteins, Disulfides, Oxidoreductases Acting on Sulfur Group Donors, Sulfur.
- chemical , physiology : Bacterial Proteins, Protein Disulfide Reductase (Glutathione).
- enzymology : Paracoccus pantotrophus.
- Amino Acid Motifs, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Dimerization, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Sequence Alignment, Sequence Homology, Amino Acid, Structure-Activity Relationship.
Abstract
The periplasmic thiol-disulfide oxidoreductase SoxS is beneficial for the sulfur-oxidizing (Sox) phenotype of the facultative chemotrophic bacterium Paracoccus pantotrophus and is not part of the Sox enzyme system. SoxS combines features of thioredoxins, glutaredoxins and the thiol-disulfide oxidoreductases of the Dsb family in structure, target specificity and reaction. The structure of SoxS was solved in oxidized and reduced forms at 2.1 and 1.9 A resolution, respectively. SoxS revealed high structural homology to typical cytoplasmic bacterial thioredoxins. In contrast, SoxS contained the active-site motif Pro-Gly-Cys-Leu-Tyr-Cys that is not present in other thioredoxins. Interestingly, the sequence of this motif is closely related to the Pro-Gly-Cys-Pro-Tyr-Cys sequence of some glutaredoxins and to the Pro-Xaa-Cys-Xaa-Tyr-Cys sequences of some members of the DsbC and DsbG subfamilies of thiol-disulfide oxidoreductases. Furthermore, the proposed substrate of SoxS, the interprotein disulfide of SoxY, Cys110(Y)-Cys110(Y), is structurally similar to oxidized glutathione. However, SoxS is proposed to specifically reduce the interprotein disulfide between two SoxY subunits, releasing a heterodimeric SoxYZ as an active part of the sulfur-oxidation cycle.
DOI: 10.1107/S0907444908043023
PubMed: 19237745
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.</title><author><name sortKey="Carius, Yvonne" sort="Carius, Yvonne" uniqKey="Carius Y" first="Yvonne" last="Carius">Yvonne Carius</name><affiliation wicri:level="3"><nlm:affiliation>Abteilung für Strukturbiologie, Zoologisches Institut, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Abteilung für Strukturbiologie, Zoologisches Institut, Christian-Albrechts-Universität zu Kiel, Kiel</wicri:regionArea><placeName><region type="land" nuts="2">Schleswig-Holstein</region><settlement type="city">Kiel</settlement></placeName></affiliation></author><author><name sortKey="Rother, Dagmar" sort="Rother, Dagmar" uniqKey="Rother D" first="Dagmar" last="Rother">Dagmar Rother</name></author><author><name sortKey="Friedrich, Cornelius G" sort="Friedrich, Cornelius G" uniqKey="Friedrich C" first="Cornelius G" last="Friedrich">Cornelius G. Friedrich</name></author><author><name sortKey="Scheidig, Axel J" sort="Scheidig, Axel J" uniqKey="Scheidig A" first="Axel J" last="Scheidig">Axel J. Scheidig</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19237745</idno><idno type="pmid">19237745</idno><idno type="doi">10.1107/S0907444908043023</idno><idno type="wicri:Area/Main/Corpus">000B20</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000B20</idno><idno type="wicri:Area/Main/Curation">000B20</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000B20</idno><idno type="wicri:Area/Main/Exploration">000B20</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.</title><author><name sortKey="Carius, Yvonne" sort="Carius, Yvonne" uniqKey="Carius Y" first="Yvonne" last="Carius">Yvonne Carius</name><affiliation wicri:level="3"><nlm:affiliation>Abteilung für Strukturbiologie, Zoologisches Institut, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Abteilung für Strukturbiologie, Zoologisches Institut, Christian-Albrechts-Universität zu Kiel, Kiel</wicri:regionArea><placeName><region type="land" nuts="2">Schleswig-Holstein</region><settlement type="city">Kiel</settlement></placeName></affiliation></author><author><name sortKey="Rother, Dagmar" sort="Rother, Dagmar" uniqKey="Rother D" first="Dagmar" last="Rother">Dagmar Rother</name></author><author><name sortKey="Friedrich, Cornelius G" sort="Friedrich, Cornelius G" uniqKey="Friedrich C" first="Cornelius G" last="Friedrich">Cornelius G. Friedrich</name></author><author><name sortKey="Scheidig, Axel J" sort="Scheidig, Axel J" uniqKey="Scheidig A" first="Axel J" last="Scheidig">Axel J. Scheidig</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="eISSN">1399-0047</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Bacterial Proteins (physiology)</term><term>Binding Sites (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Dimerization (MeSH)</term><term>Disulfides (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases Acting on Sulfur Group Donors (metabolism)</term><term>Paracoccus pantotrophus (enzymology)</term><term>Protein Conformation (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (chemistry)</term><term>Protein Disulfide Reductase (Glutathione) (physiology)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Selenomethionine (chemistry)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Structure-Activity Relationship (MeSH)</term><term>Sulfur (metabolism)</term><term>Thioredoxins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Dimérisation (MeSH)</term><term>Disulfures (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Modèles moléculaires (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Oxidoreductases acting on sulfur group donors (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Paracoccus pantotrophus (enzymologie)</term><term>Protein-disulfide reductase (glutathione) (composition chimique)</term><term>Protein-disulfide reductase (glutathione) (physiologie)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines bactériennes (physiologie)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Relation structure-activité (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Soufre (métabolisme)</term><term>Sélénométhionine (composition chimique)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thiorédoxines (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Recombinant Fusion Proteins</term><term>Selenomethionine</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Disulfides</term><term>Oxidoreductases Acting on Sulfur Group Donors</term><term>Sulfur</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Bacterial Proteins</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Protein-disulfide reductase (glutathione)</term><term>Protéines bactériennes</term><term>Protéines de fusion recombinantes</term><term>Sélénométhionine</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Paracoccus pantotrophus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Paracoccus pantotrophus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Oxidoreductases acting on sulfur group donors</term><term>Protéines bactériennes</term><term>Soufre</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protein-disulfide reductase (glutathione)</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Dimerization</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Oxydoréduction</term><term>Relation structure-activité</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The periplasmic thiol-disulfide oxidoreductase SoxS is beneficial for the sulfur-oxidizing (Sox) phenotype of the facultative chemotrophic bacterium Paracoccus pantotrophus and is not part of the Sox enzyme system. SoxS combines features of thioredoxins, glutaredoxins and the thiol-disulfide oxidoreductases of the Dsb family in structure, target specificity and reaction. The structure of SoxS was solved in oxidized and reduced forms at 2.1 and 1.9 A resolution, respectively. SoxS revealed high structural homology to typical cytoplasmic bacterial thioredoxins. In contrast, SoxS contained the active-site motif Pro-Gly-Cys-Leu-Tyr-Cys that is not present in other thioredoxins. Interestingly, the sequence of this motif is closely related to the Pro-Gly-Cys-Pro-Tyr-Cys sequence of some glutaredoxins and to the Pro-Xaa-Cys-Xaa-Tyr-Cys sequences of some members of the DsbC and DsbG subfamilies of thiol-disulfide oxidoreductases. Furthermore, the proposed substrate of SoxS, the interprotein disulfide of SoxY, Cys110(Y)-Cys110(Y), is structurally similar to oxidized glutathione. However, SoxS is proposed to specifically reduce the interprotein disulfide between two SoxY subunits, releasing a heterodimeric SoxYZ as an active part of the sulfur-oxidation cycle.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19237745</PMID><DateCompleted><Year>2009</Year><Month>07</Month><Day>17</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1399-0047</ISSN><JournalIssue CitedMedium="Internet"><Volume>65</Volume><Issue>Pt 3</Issue><PubDate><Year>2009</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.</ArticleTitle><Pagination><MedlinePgn>229-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S0907444908043023</ELocationID><Abstract><AbstractText>The periplasmic thiol-disulfide oxidoreductase SoxS is beneficial for the sulfur-oxidizing (Sox) phenotype of the facultative chemotrophic bacterium Paracoccus pantotrophus and is not part of the Sox enzyme system. SoxS combines features of thioredoxins, glutaredoxins and the thiol-disulfide oxidoreductases of the Dsb family in structure, target specificity and reaction. The structure of SoxS was solved in oxidized and reduced forms at 2.1 and 1.9 A resolution, respectively. SoxS revealed high structural homology to typical cytoplasmic bacterial thioredoxins. In contrast, SoxS contained the active-site motif Pro-Gly-Cys-Leu-Tyr-Cys that is not present in other thioredoxins. Interestingly, the sequence of this motif is closely related to the Pro-Gly-Cys-Pro-Tyr-Cys sequence of some glutaredoxins and to the Pro-Xaa-Cys-Xaa-Tyr-Cys sequences of some members of the DsbC and DsbG subfamilies of thiol-disulfide oxidoreductases. Furthermore, the proposed substrate of SoxS, the interprotein disulfide of SoxY, Cys110(Y)-Cys110(Y), is structurally similar to oxidized glutathione. However, SoxS is proposed to specifically reduce the interprotein disulfide between two SoxY subunits, releasing a heterodimeric SoxYZ as an active part of the sulfur-oxidation cycle.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Carius</LastName><ForeName>Yvonne</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Abteilung für Strukturbiologie, Zoologisches Institut, Christian-Albrechts-Universität zu Kiel, Kiel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rother</LastName><ForeName>Dagmar</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Friedrich</LastName><ForeName>Cornelius G</ForeName><Initials>CG</Initials></Author><Author ValidYN="Y"><LastName>Scheidig</LastName><ForeName>Axel J</ForeName><Initials>AJ</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>3D4T</AccessionNumber><AccessionNumber>3DML</AccessionNumber><AccessionNumber>R3D4TSF</AccessionNumber><AccessionNumber>R3DMLSF</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>02</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol Crystallogr</MedlineTA><NlmUniqueID>9305878</NlmUniqueID><ISSNLinking>0907-4449</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>964MRK2PEL</RegistryNumber><NameOfSubstance UI="D012645">Selenomethionine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="D050862">Oxidoreductases Acting on Sulfur Group Donors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.-</RegistryNumber><NameOfSubstance UI="C413329">SoxZ protein, Paracoccus pantotrophus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050862" MajorTopicYN="N">Oxidoreductases Acting on Sulfur Group Donors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042084" MajorTopicYN="N">Paracoccus pantotrophus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012645" MajorTopicYN="N">Selenomethionine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2008</Year><Month>09</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2008</Year><Month>12</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>2</Month><Day>25</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>2</Month><Day>25</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>7</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19237745</ArticleId><ArticleId IdType="pii">S0907444908043023</ArticleId><ArticleId IdType="doi">10.1107/S0907444908043023</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Schleswig-Holstein</li></region><settlement><li>Kiel</li></settlement></list><tree><noCountry><name sortKey="Friedrich, Cornelius G" sort="Friedrich, Cornelius G" uniqKey="Friedrich C" first="Cornelius G" last="Friedrich">Cornelius G. Friedrich</name><name sortKey="Rother, Dagmar" sort="Rother, Dagmar" uniqKey="Rother D" first="Dagmar" last="Rother">Dagmar Rother</name><name sortKey="Scheidig, Axel J" sort="Scheidig, Axel J" uniqKey="Scheidig A" first="Axel J" last="Scheidig">Axel J. Scheidig</name></noCountry><country name="Allemagne"><region name="Schleswig-Holstein"><name sortKey="Carius, Yvonne" sort="Carius, Yvonne" uniqKey="Carius Y" first="Yvonne" last="Carius">Yvonne Carius</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000A71 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000A71 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:19237745
|texte= The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:19237745" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |