Structure of glutaredoxin Grx1p C30S mutant from yeast.
Identifieur interne : 000C54 ( Main/Exploration ); précédent : 000C53; suivant : 000C55Structure of glutaredoxin Grx1p C30S mutant from yeast.
Auteurs : Kjell O. H Kansson [Danemark] ; Jakob R. WintherSource :
- Acta crystallographica. Section D, Biological crystallography [ 0907-4449 ] ; 2007.
Descripteurs français
- KwdFr :
- Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Glutathion (génétique), Glutathion (métabolisme), Modèles moléculaires (MeSH), Mutation (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Pliage des protéines (MeSH), Protéines bactériennes (génétique), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines luminescentes (génétique), Sites de fixation (MeSH), Spectroscopie par résonance magnétique (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Oxidoreductases, Protéines de Saccharomyces cerevisiae, Protéines de fusion recombinantes.
- génétique : Glutathion, Oxidoreductases, Protéines bactériennes, Protéines de Saccharomyces cerevisiae, Protéines de fusion recombinantes, Protéines luminescentes.
- métabolisme : Glutathion, Oxidoreductases, Protéines de Saccharomyces cerevisiae.
- Cristallographie aux rayons X, Données de séquences moléculaires, Glutarédoxines, Modèles moléculaires, Mutation, Pliage des protéines, Sites de fixation, Spectroscopie par résonance magnétique, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (genetics), Binding Sites (MeSH), Conserved Sequence (MeSH), Crystallography, X-Ray (MeSH), Glutaredoxins (MeSH), Glutathione (genetics), Glutathione (metabolism), Luminescent Proteins (genetics), Magnetic Resonance Spectroscopy (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Protein Folding (MeSH), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , chemistry : Oxidoreductases, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Bacterial Proteins, Glutathione, Luminescent Proteins, Oxidoreductases, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutathione, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- Amino Acid Sequence, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Glutaredoxins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Mutation, Protein Folding.
Abstract
Glutathionylated glutaredoxin Grx1p C30S mutant from yeast has been crystallized in space group C222(1) and a fusion protein between redox-sensitive yellow fluorescent protein (rxYFP) and Grx1p C30S has been crystallized in space group P6(4). The structure of the latter was solved by molecular replacement using the known rxYFP structure as a search model. The structure of the Grx1p moiety was built and the structure was refined against 2.7 A synchrotron data to an R(free) of 25.7%. There are no specific contacts between the two domains, indicating that the observed enhanced exchange of reduction equivalents between them arises from diffusion or from an enhanced collision rate in solution. The Grx1p structure thus obtained was subsequently used to solve the structure of the orthorhombic crystal, which could be refined against 2.0 A data to an R(free) of 24.3%. The structure of the glutathione-bound protein and the glutaredoxin domain in the fusion protein are similar. The covalent disulfide bond between the glutathione and protein is broken upon exposure to synchrotron radiation. The structure and the glutathione-binding mode are described and compared with existing crystallographic and nuclear magnetic resonance (NMR) structures of related glutaredoxins. Conserved residues are clustered on one side of the active site.
DOI: 10.1107/S0907444906051675
PubMed: 17327665
Affiliations:
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Winther</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17327665</idno><idno type="pmid">17327665</idno><idno type="doi">10.1107/S0907444906051675</idno><idno type="wicri:Area/Main/Corpus">000C77</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C77</idno><idno type="wicri:Area/Main/Curation">000C77</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C77</idno><idno type="wicri:Area/Main/Exploration">000C77</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structure of glutaredoxin Grx1p C30S mutant from yeast.</title><author><name sortKey="H Kansson, Kjell O" sort="H Kansson, Kjell O" uniqKey="H Kansson K" first="Kjell O" last="H Kansson">Kjell O. H Kansson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø, Denmark. kohakansson@aki.ku.dk</nlm:affiliation><country xml:lang="fr">Danemark</country><wicri:regionArea>Department of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø</wicri:regionArea><wicri:noRegion>DK-2100 Copenhagen Ø</wicri:noRegion></affiliation></author><author><name sortKey="Winther, Jakob R" sort="Winther, Jakob R" uniqKey="Winther J" first="Jakob R" last="Winther">Jakob R. Winther</name></author></analytic><series><title level="j">Acta crystallographica. Section D, Biological crystallography</title><idno type="ISSN">0907-4449</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Bacterial Proteins (genetics)</term><term>Binding Sites (MeSH)</term><term>Conserved Sequence (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (genetics)</term><term>Glutathione (metabolism)</term><term>Luminescent Proteins (genetics)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Protein Folding (MeSH)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (chemistry)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cristallographie aux rayons X (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (génétique)</term><term>Glutathion (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Pliage des protéines (MeSH)</term><term>Protéines bactériennes (génétique)</term><term>Protéines de Saccharomyces cerevisiae (composition chimique)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines luminescentes (génétique)</term><term>Sites de fixation (MeSH)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Séquence conservée (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term><term>Recombinant Fusion Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Glutathione</term><term>Luminescent Proteins</term><term>Oxidoreductases</term><term>Recombinant Fusion Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Oxidoreductases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutathion</term><term>Oxidoreductases</term><term>Protéines bactériennes</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de fusion recombinantes</term><term>Protéines luminescentes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Oxidoreductases</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Conserved Sequence</term><term>Crystallography, X-Ray</term><term>Glutaredoxins</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Protein Folding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Modèles moléculaires</term><term>Mutation</term><term>Pliage des protéines</term><term>Sites de fixation</term><term>Spectroscopie par résonance magnétique</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathionylated glutaredoxin Grx1p C30S mutant from yeast has been crystallized in space group C222(1) and a fusion protein between redox-sensitive yellow fluorescent protein (rxYFP) and Grx1p C30S has been crystallized in space group P6(4). The structure of the latter was solved by molecular replacement using the known rxYFP structure as a search model. The structure of the Grx1p moiety was built and the structure was refined against 2.7 A synchrotron data to an R(free) of 25.7%. There are no specific contacts between the two domains, indicating that the observed enhanced exchange of reduction equivalents between them arises from diffusion or from an enhanced collision rate in solution. The Grx1p structure thus obtained was subsequently used to solve the structure of the orthorhombic crystal, which could be refined against 2.0 A data to an R(free) of 24.3%. The structure of the glutathione-bound protein and the glutaredoxin domain in the fusion protein are similar. The covalent disulfide bond between the glutathione and protein is broken upon exposure to synchrotron radiation. The structure and the glutathione-binding mode are described and compared with existing crystallographic and nuclear magnetic resonance (NMR) structures of related glutaredoxins. Conserved residues are clustered on one side of the active site.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17327665</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>05</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0907-4449</ISSN><JournalIssue CitedMedium="Print"><Volume>63</Volume><Issue>Pt 3</Issue><PubDate><Year>2007</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Biological crystallography</Title><ISOAbbreviation>Acta Crystallogr D Biol Crystallogr</ISOAbbreviation></Journal><ArticleTitle>Structure of glutaredoxin Grx1p C30S mutant from yeast.</ArticleTitle><Pagination><MedlinePgn>288-94</MedlinePgn></Pagination><Abstract><AbstractText>Glutathionylated glutaredoxin Grx1p C30S mutant from yeast has been crystallized in space group C222(1) and a fusion protein between redox-sensitive yellow fluorescent protein (rxYFP) and Grx1p C30S has been crystallized in space group P6(4). The structure of the latter was solved by molecular replacement using the known rxYFP structure as a search model. The structure of the Grx1p moiety was built and the structure was refined against 2.7 A synchrotron data to an R(free) of 25.7%. There are no specific contacts between the two domains, indicating that the observed enhanced exchange of reduction equivalents between them arises from diffusion or from an enhanced collision rate in solution. The Grx1p structure thus obtained was subsequently used to solve the structure of the orthorhombic crystal, which could be refined against 2.0 A data to an R(free) of 24.3%. The structure of the glutathione-bound protein and the glutaredoxin domain in the fusion protein are similar. The covalent disulfide bond between the glutathione and protein is broken upon exposure to synchrotron radiation. The structure and the glutathione-binding mode are described and compared with existing crystallographic and nuclear magnetic resonance (NMR) structures of related glutaredoxins. Conserved residues are clustered on one side of the active site.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Håkansson</LastName><ForeName>Kjell O</ForeName><Initials>KO</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology, August Krogh Building, University of Copenhagen, Universitetsparken 13, DK-2100 Copenhagen Ø, Denmark. kohakansson@aki.ku.dk</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Winther</LastName><ForeName>Jakob R</ForeName><Initials>JR</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>02</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Biol 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MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008164" MajorTopicYN="N">Luminescent Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></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="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName 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PubStatus="received"><Year>2006</Year><Month>10</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>11</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>3</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>4</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>3</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17327665</ArticleId><ArticleId IdType="pii">S0907444906051675</ArticleId><ArticleId IdType="doi">10.1107/S0907444906051675</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Danemark</li></country></list><tree><noCountry><name sortKey="Winther, Jakob R" sort="Winther, Jakob R" uniqKey="Winther J" first="Jakob R" last="Winther">Jakob R. Winther</name></noCountry><country name="Danemark"><noRegion><name sortKey="H Kansson, Kjell O" sort="H Kansson, Kjell O" uniqKey="H Kansson K" first="Kjell O" last="H Kansson">Kjell O. H Kansson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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