Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.
Identifieur interne : 001010 ( Main/Exploration ); précédent : 001009; suivant : 001011Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.
Auteurs : B. Xia [États-Unis] ; A. Vlamis-Gardikas ; A. Holmgren ; P E Wright ; H J DysonSource :
- Journal of molecular biology [ 0022-2836 ] ; 2001.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Cystéine (métabolisme), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (enzymologie), Glutarédoxines (MeSH), Glutathione transferase (classification), Glutathione transferase (composition chimique), Humains (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines (métabolisme), Résonance magnétique nucléaire biomoléculaire (MeSH), Sites de fixation (MeSH), Solutions (MeSH), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Évolution moléculaire (MeSH).
- MESH :
- classification : Glutathione transferase.
- composition chimique : Glutathione transferase, Protéines.
- enzymologie : Escherichia coli.
- métabolisme : Cystéine, Disulfures, Protéines.
- Alignement de séquences, Animaux, Données de séquences moléculaires, Glutarédoxines, Humains, Modèles moléculaires, Oxidoreductases, Oxydoréduction, Résonance magnétique nucléaire biomoléculaire, Sites de fixation, Solutions, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Binding Sites (MeSH), Cysteine (metabolism), Disulfides (metabolism), Escherichia coli (enzymology), Evolution, Molecular (MeSH), Glutaredoxins (MeSH), Glutathione Transferase (chemistry), Glutathione Transferase (classification), Humans (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Proteins (chemistry), Proteins (metabolism), Sequence Alignment (MeSH), Solutions (MeSH).
- MESH :
- chemical , chemistry : Glutathione Transferase, Proteins.
- chemical , classification : Glutathione Transferase.
- chemical , metabolism : Cysteine, Disulfides, Proteins.
- enzymology : Escherichia coli.
- Amino Acid Sequence, Animals, Binding Sites, Evolution, Molecular, Glutaredoxins, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Oxidoreductases, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment, Solutions.
Abstract
Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence identity and lack of electron donor activity with ribonucleotide reductase. However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses.
DOI: 10.1006/jmbi.2001.4721
PubMed: 11453697
Affiliations:
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Holmgren</name></author><author><name sortKey="Wright, P E" sort="Wright, P E" uniqKey="Wright P" first="P E" last="Wright">P E Wright</name></author><author><name sortKey="Dyson, H J" sort="Dyson, H J" uniqKey="Dyson H" first="H J" last="Dyson">H J Dyson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2001">2001</date><idno type="RBID">pubmed:11453697</idno><idno type="pmid">11453697</idno><idno type="doi">10.1006/jmbi.2001.4721</idno><idno type="wicri:Area/Main/Corpus">001023</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001023</idno><idno type="wicri:Area/Main/Curation">001023</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001023</idno><idno type="wicri:Area/Main/Exploration">001023</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.</title><author><name sortKey="Xia, B" sort="Xia, B" uniqKey="Xia B" first="B" last="Xia">B. 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However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11453697</PMID><DateCompleted><Year>2001</Year><Month>08</Month><Day>09</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>310</Volume><Issue>4</Issue><PubDate><Year>2001</Year><Month>Jul</Month><Day>20</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases.</ArticleTitle><Pagination><MedlinePgn>907-18</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxin 2 (Grx2) from Escherichia coli is distinguished from other glutaredoxins by its larger size, low overall sequence identity and lack of electron donor activity with ribonucleotide reductase. However, catalysis of glutathione (GSH)-dependent general disulfide reduction by Grx2 is extremely efficient. The high-resolution solution structure of E. coli Grx2 shows a two-domain protein, with residues 1 to 72 forming a classical "thioredoxin-fold" glutaredoxin domain, connected by an 11 residue linker to the highly helical C-terminal domain, residues 84 to 215. The active site, Cys9-Pro10-Tyr11-Cys12, is buried in the interface between the two domains, but Cys9 is solvent-accessible, consistent with its role in catalysis. The structures reveal the hither to unknown fact that Grx2 is structurally similar to glutathione-S-transferases (GST), although there is no obvious sequence homology. The similarity of these structures gives important insights into the functional significance of a new class of mammalian GST-like proteins, the single-cysteine omega class, which have glutaredoxin oxidoreductase activity rather than GSH-S-transferase conjugating activity. E. coli Grx 2 is structurally and functionally a member of this new expanding family of large glutaredoxins. The primary function of Grx2 as a GST-like glutaredoxin is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including stress responses.</AbstractText><CopyrightInformation>Copyright 2001 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xia</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Molecular Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vlamis-Gardikas</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Wright</LastName><ForeName>P E</ForeName><Initials>PE</Initials></Author><Author ValidYN="Y"><LastName>Dyson</LastName><ForeName>H 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UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012996">Solutions</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</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="D019906" MajorTopicYN="N">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" 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PubStatus="pubmed"><Year>2001</Year><Month>7</Month><Day>17</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>8</Month><Day>10</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>7</Month><Day>17</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11453697</ArticleId><ArticleId IdType="doi">10.1006/jmbi.2001.4721</ArticleId><ArticleId IdType="pii">S0022-2836(01)94721-7</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Dyson, H J" sort="Dyson, H J" uniqKey="Dyson H" first="H J" last="Dyson">H J Dyson</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Vlamis Gardikas, A" sort="Vlamis Gardikas, A" uniqKey="Vlamis Gardikas A" first="A" last="Vlamis-Gardikas">A. Vlamis-Gardikas</name><name sortKey="Wright, P E" sort="Wright, P E" uniqKey="Wright P" first="P E" last="Wright">P E Wright</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Xia, B" sort="Xia, B" uniqKey="Xia B" first="B" last="Xia">B. Xia</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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