Structural basis for target protein recognition by the protein disulfide reductase thioredoxin.
Identifieur interne : 000D11 ( Main/Exploration ); précédent : 000D10; suivant : 000D12Structural basis for target protein recognition by the protein disulfide reductase thioredoxin.
Auteurs : Kenji Maeda [Danemark] ; Per H Gglund ; Christine Finnie ; Birte Svensson ; Anette HenriksenSource :
- Structure (London, England : 1993) [ 0969-2126 ] ; 2006.
Descripteurs français
- KwdFr :
- Conformation moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Cystéine (composition chimique), Disulfures (composition chimique), Glutarédoxines (MeSH), Glutathion (composition chimique), Glutathione transferase (composition chimique), Glutathione transferase (métabolisme), Hordeum (MeSH), Modèles chimiques (MeSH), Modèles moléculaires (MeSH), Motifs d'acides aminés (MeSH), Oxidoreductases (composition chimique), Pliage des protéines (MeSH), Protein-disulfide reductase (glutathione) (composition chimique), Protéines (composition chimique), Thiorédoxines (composition chimique).
- MESH :
- composition chimique : Cystéine, Disulfures, Glutathion, Glutathione transferase, Oxidoreductases, Protein-disulfide reductase (glutathione), Protéines, Thiorédoxines.
- métabolisme : Glutathione transferase.
- Conformation moléculaire, Cristallographie aux rayons X, Glutarédoxines, Hordeum, Modèles chimiques, Modèles moléculaires, Motifs d'acides aminés, Pliage des protéines.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Crystallography, X-Ray (MeSH), Cysteine (chemistry), Disulfides (chemistry), Glutaredoxins (MeSH), Glutathione (chemistry), Glutathione Transferase (chemistry), Glutathione Transferase (metabolism), Hordeum (MeSH), Models, Chemical (MeSH), Models, Molecular (MeSH), Molecular Conformation (MeSH), Oxidoreductases (chemistry), Protein Disulfide Reductase (Glutathione) (chemistry), Protein Folding (MeSH), Proteins (chemistry), Thioredoxins (chemistry).
- MESH :
- chemical , chemistry : Cysteine, Disulfides, Glutathione, Glutathione Transferase, Oxidoreductases, Protein Disulfide Reductase (Glutathione), Proteins, Thioredoxins.
- chemical , metabolism : Glutathione Transferase.
- Amino Acid Motifs, Crystallography, X-Ray, Glutaredoxins, Hordeum, Models, Chemical, Models, Molecular, Molecular Conformation, Protein Folding.
Abstract
Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.
DOI: 10.1016/j.str.2006.09.012
PubMed: 17098195
Affiliations:
Links toward previous steps (curation, corpus...)
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Lyngby</wicri:noRegion></affiliation></author><author><name sortKey="H Gglund, Per" sort="H Gglund, Per" uniqKey="H Gglund P" first="Per" last="H Gglund">Per H Gglund</name></author><author><name sortKey="Finnie, Christine" sort="Finnie, Christine" uniqKey="Finnie C" first="Christine" last="Finnie">Christine Finnie</name></author><author><name sortKey="Svensson, Birte" sort="Svensson, Birte" uniqKey="Svensson B" first="Birte" last="Svensson">Birte Svensson</name></author><author><name sortKey="Henriksen, Anette" sort="Henriksen, Anette" uniqKey="Henriksen A" first="Anette" last="Henriksen">Anette Henriksen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:17098195</idno><idno type="pmid">17098195</idno><idno type="doi">10.1016/j.str.2006.09.012</idno><idno type="wicri:Area/Main/Corpus">000D00</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D00</idno><idno type="wicri:Area/Main/Curation">000D00</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D00</idno><idno type="wicri:Area/Main/Exploration">000D00</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structural basis for target protein recognition by the protein disulfide reductase thioredoxin.</title><author><name sortKey="Maeda, Kenji" sort="Maeda, Kenji" uniqKey="Maeda K" first="Kenji" last="Maeda">Kenji Maeda</name><affiliation wicri:level="1"><nlm:affiliation>Enzyme and Protein Chemistry, BioCentrum-DTU, Søltofts Plads, Building 224, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark.</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Enzyme and Protein Chemistry, BioCentrum-DTU, Søltofts Plads, Building 224, Technical University of Denmark, DK-2800 Kgs. Lyngby</wicri:regionArea><wicri:noRegion>DK-2800 Kgs. Lyngby</wicri:noRegion></affiliation></author><author><name sortKey="H Gglund, Per" sort="H Gglund, Per" uniqKey="H Gglund P" first="Per" last="H Gglund">Per H Gglund</name></author><author><name sortKey="Finnie, Christine" sort="Finnie, Christine" uniqKey="Finnie C" first="Christine" last="Finnie">Christine Finnie</name></author><author><name sortKey="Svensson, Birte" sort="Svensson, Birte" uniqKey="Svensson B" first="Birte" last="Svensson">Birte Svensson</name></author><author><name sortKey="Henriksen, Anette" sort="Henriksen, Anette" uniqKey="Henriksen A" first="Anette" last="Henriksen">Anette Henriksen</name></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="ISSN">0969-2126</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Cysteine (chemistry)</term><term>Disulfides (chemistry)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (chemistry)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (metabolism)</term><term>Hordeum (MeSH)</term><term>Models, Chemical (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Conformation (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Protein Disulfide Reductase (Glutathione) (chemistry)</term><term>Protein Folding (MeSH)</term><term>Proteins (chemistry)</term><term>Thioredoxins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation moléculaire (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cystéine (composition chimique)</term><term>Disulfures (composition chimique)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Glutathione transferase (composition chimique)</term><term>Glutathione transferase (métabolisme)</term><term>Hordeum (MeSH)</term><term>Modèles chimiques (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Pliage des protéines (MeSH)</term><term>Protein-disulfide reductase (glutathione) (composition chimique)</term><term>Protéines (composition chimique)</term><term>Thiorédoxines (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Disulfides</term><term>Glutathione</term><term>Glutathione Transferase</term><term>Oxidoreductases</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Disulfures</term><term>Glutathion</term><term>Glutathione transferase</term><term>Oxidoreductases</term><term>Protein-disulfide reductase (glutathione)</term><term>Protéines</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathione transferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Crystallography, X-Ray</term><term>Glutaredoxins</term><term>Hordeum</term><term>Models, Chemical</term><term>Models, Molecular</term><term>Molecular Conformation</term><term>Protein Folding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation moléculaire</term><term>Cristallographie aux rayons X</term><term>Glutarédoxines</term><term>Hordeum</term><term>Modèles chimiques</term><term>Modèles moléculaires</term><term>Motifs d'acides aminés</term><term>Pliage des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17098195</PMID><DateCompleted><Year>2007</Year><Month>01</Month><Day>16</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0969-2126</ISSN><JournalIssue CitedMedium="Print"><Volume>14</Volume><Issue>11</Issue><PubDate><Year>2006</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Structure (London, England : 1993)</Title><ISOAbbreviation>Structure</ISOAbbreviation></Journal><ArticleTitle>Structural basis for target protein recognition by the protein disulfide reductase thioredoxin.</ArticleTitle><Pagination><MedlinePgn>1701-10</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. 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States</Country><MedlineTA>Structure</MedlineTA><NlmUniqueID>101087697</NlmUniqueID><ISSNLinking>0969-2126</ISSNLinking></MedlineJournalInfo><ChemicalList><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="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" 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MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>08</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>09</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>09</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>11</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>1</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>11</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17098195</ArticleId><ArticleId IdType="pii">S0969-2126(06)00398-4</ArticleId><ArticleId IdType="doi">10.1016/j.str.2006.09.012</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Danemark</li></country></list><tree><noCountry><name sortKey="Finnie, Christine" sort="Finnie, Christine" uniqKey="Finnie C" first="Christine" last="Finnie">Christine Finnie</name><name sortKey="H Gglund, Per" sort="H Gglund, Per" uniqKey="H Gglund P" first="Per" last="H Gglund">Per H Gglund</name><name sortKey="Henriksen, Anette" sort="Henriksen, Anette" uniqKey="Henriksen A" first="Anette" last="Henriksen">Anette Henriksen</name><name sortKey="Svensson, Birte" sort="Svensson, Birte" uniqKey="Svensson B" first="Birte" last="Svensson">Birte Svensson</name></noCountry><country name="Danemark"><noRegion><name sortKey="Maeda, Kenji" sort="Maeda, Kenji" uniqKey="Maeda K" first="Kenji" last="Maeda">Kenji Maeda</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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