NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.
Identifieur interne : 001099 ( Main/Exploration ); précédent : 001098; suivant : 001100NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.
Auteurs : K. Nordstrand [Suède] ; F. Slund ; A. Holmgren ; G. Otting ; K D BerndtSource :
- Journal of molecular biology [ 0022-2836 ] ; 1999.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Catalyse (MeSH), Conformation des protéines (MeSH), Cystéine (composition chimique), Données de séquences moléculaires (MeSH), Escherichia coli (composition chimique), Escherichia coli (génétique), Glutarédoxines (MeSH), Humains (MeSH), Modèles biologiques (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines (génétique), Protéines (métabolisme), Protéines bactériennes (composition chimique), Protéines bactériennes (métabolisme), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (métabolisme), Relation structure-activité (MeSH), Ribonucleotide reductases (métabolisme), Similitude de séquences d'acides aminés (MeSH), Spectroscopie par résonance magnétique (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Cystéine, Escherichia coli, Protéines, Protéines bactériennes, Protéines de fusion recombinantes.
- génétique : Escherichia coli, Protéines.
- métabolisme : Protéines, Protéines bactériennes, Protéines de fusion recombinantes, Ribonucleotide reductases.
- Alignement de séquences, Catalyse, Conformation des protéines, Données de séquences moléculaires, Glutarédoxines, Humains, Modèles biologiques, Modèles moléculaires, Mutagenèse dirigée, Oxidoreductases, Oxydoréduction, Relation structure-activité, Similitude de séquences d'acides aminés, Spectroscopie par résonance magnétique, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Catalysis (MeSH), Cysteine (chemistry), Escherichia coli (chemistry), Escherichia coli (genetics), Glutaredoxins (MeSH), Humans (MeSH), Magnetic Resonance Spectroscopy (MeSH), Models, Biological (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Proteins (chemistry), Proteins (genetics), Proteins (metabolism), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (metabolism), Ribonucleotide Reductases (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH), Structure-Activity Relationship (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Bacterial Proteins, Cysteine, Proteins, Recombinant Fusion Proteins.
- chemical , genetics : Proteins.
- chemical , metabolism : Bacterial Proteins, Proteins, Recombinant Fusion Proteins, Ribonucleotide Reductases.
- chemistry : Escherichia coli.
- genetics : Escherichia coli.
- Amino Acid Sequence, Catalysis, Glutaredoxins, Humans, Magnetic Resonance Spectroscopy, Models, Biological, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Oxidation-Reduction, Oxidoreductases, Protein Conformation, Sequence Alignment, Sequence Homology, Amino Acid, Structure-Activity Relationship, Substrate Specificity.
Abstract
Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with a well-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in the reduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family.
DOI: 10.1006/jmbi.1998.2444
PubMed: 9973569
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Nordstrand</name><affiliation wicri:level="3"><nlm:affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Slund, F" sort="Slund, F" uniqKey="Slund F" first="F" last="Slund">F. Slund</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Otting, G" sort="Otting, G" uniqKey="Otting G" first="G" last="Otting">G. 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(MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (genetics)</term><term>Proteins (metabolism)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Ribonucleotide Reductases (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Structure-Activity Relationship (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Catalyse (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Cystéine (composition chimique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (composition chimique)</term><term>Escherichia coli (génétique)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Modèles 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biologiques</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Relation structure-activité</term><term>Similitude de séquences d'acides aminés</term><term>Spectroscopie par résonance magnétique</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with a well-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in the reduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9973569</PMID><DateCompleted><Year>1999</Year><Month>04</Month><Day>01</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>286</Volume><Issue>2</Issue><PubDate><Year>1999</Year><Month>Feb</Month><Day>19</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>NMR structure of Escherichia coli glutaredoxin 3-glutathione mixed disulfide complex: implications for the enzymatic mechanism.</ArticleTitle><Pagination><MedlinePgn>541-52</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (Grxs) catalyze reversible oxidation/reduction of protein disulfide groups and glutathione-containing mixed disulfide groups via an active site Grx-glutathione mixed disulfide (Grx-SG) intermediate. The NMR solution structure of the Escherichia coli Grx3 mixed disulfide with glutathione (Grx3-SG) was determined using a C14S mutant which traps this intermediate in the redox reaction. The structure contains a thioredoxin fold, with a well-defined binding site for glutathione which involves two intermolecular backbone-backbone hydrogen bonds forming an antiparallel intermolecular beta-bridge between the protein and glutathione. The solution structure of E. coli Grx3-SG also suggests a binding site for a second glutathione in the reduction of the Grx3-SG intermediate, which is consistent with the specificity of reduction observed in Grxs. Molecular details of the structure in relation to the stability of the intermediate and the activity of Grx3 as a reductant of glutathione mixed disulfide groups are discussed. A comparison of glutathione binding in Grx3-SG and ligand binding in other members of the thioredoxin superfamily is presented, which illustrates the highly conserved intermolecular interactions in this protein family.</AbstractText><CopyrightInformation>Copyright 1998 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nordstrand</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institute, S-171 77, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>slund</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Otting</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>K D</ForeName><Initials>KD</Initials></Author></AuthorList><Language>eng</Language><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></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX 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="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.4.-</RegistryNumber><NameOfSubstance UI="D012264">Ribonucleotide Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><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></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="Y">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</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="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="Y">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</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="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>2</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>2</Month><Day>12</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>2</Month><Day>12</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9973569</ArticleId><ArticleId IdType="pii">S0022283698924445</ArticleId><ArticleId IdType="doi">10.1006/jmbi.1998.2444</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Berndt, K D" sort="Berndt, K D" uniqKey="Berndt K" first="K D" last="Berndt">K D Berndt</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Otting, G" sort="Otting, G" uniqKey="Otting G" first="G" last="Otting">G. Otting</name><name sortKey="Slund, F" sort="Slund, F" uniqKey="Slund F" first="F" last="Slund">F. Slund</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Nordstrand, K" sort="Nordstrand, K" uniqKey="Nordstrand K" first="K" last="Nordstrand">K. Nordstrand</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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