The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.
Identifieur interne : 001240 ( Main/Exploration ); précédent : 001239; suivant : 001241The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.
Auteurs : J H Bushweller [Suisse] ; M. Billeter ; A. Holmgren ; K. WüthrichSource :
- Journal of molecular biology [ 0022-2836 ] ; 1994.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Cystéine (MeSH), Disulfures (composition chimique), Données de séquences moléculaires (MeSH), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Glutathion (composition chimique), Glutathion (métabolisme), Liaison hydrogène (MeSH), Modèles moléculaires (MeSH), Mutation ponctuelle (MeSH), Oxidoreductases (MeSH), Pliage des protéines (MeSH), Protéines (composition chimique), Protéines (métabolisme), Protéines bactériennes (MeSH), Sites de fixation (MeSH), Solutions (MeSH), Spectroscopie par résonance magnétique (méthodes), Structure secondaire des protéines (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Disulfures, Glutathion, Protéines.
- métabolisme : Escherichia coli, Glutathion, Protéines.
- méthodes : Spectroscopie par résonance magnétique.
- Conformation des protéines, Cristallographie aux rayons X, Cystéine, Données de séquences moléculaires, Glutarédoxines, Liaison hydrogène, Modèles moléculaires, Mutation ponctuelle, Oxidoreductases, Pliage des protéines, Protéines bactériennes, Sites de fixation, Solutions, Structure secondaire des protéines, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (MeSH), Binding Sites (MeSH), Conserved Sequence (MeSH), Crystallography, X-Ray (MeSH), Cysteine (MeSH), Disulfides (chemistry), Escherichia coli (metabolism), Glutaredoxins (MeSH), Glutathione (chemistry), Glutathione (metabolism), Hydrogen Bonding (MeSH), Magnetic Resonance Spectroscopy (methods), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidoreductases (MeSH), Point Mutation (MeSH), Protein Conformation (MeSH), Protein Folding (MeSH), Protein Structure, Secondary (MeSH), Proteins (chemistry), Proteins (metabolism), Solutions (MeSH).
- MESH :
- chemical , chemistry : Disulfides, Glutathione, Proteins.
- chemical , metabolism : Glutathione, Proteins.
- chemical : Bacterial Proteins, Cysteine, Glutaredoxins, Oxidoreductases, Solutions.
- metabolism : Escherichia coli.
- methods : Magnetic Resonance Spectroscopy.
- Amino Acid Sequence, Binding Sites, Conserved Sequence, Crystallography, X-Ray, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Point Mutation, Protein Conformation, Protein Folding, Protein Structure, Secondary.
Abstract
The determination of the nuclear magnetic resonance (NMR) solution structured of the mixed disulfide between the mutant Escherichia coli glutaredoxin Grx(C14S) and glutathione (GSH), Grx(C14S)-SG, is described, the binding site for GSH on Grx(C14S) is located, and the non-bonding interactions between -SG and the protein are characterized. Based on nearly complete sequence-specific NMR assignments, 1010 nuclear Overhauser enhancement upper distance constraints and 116 dihedral angle constraints were obtained as the input for the structure calculations, for which the distance geometry program DIANA was used followed by energy minimization in a waterbath with the AMBER force field in the program OPAL. The -SG moiety was found to be localized on the surface of the protein in a cleft bounded by the amino acid residues Y13, T58, V59, Y72, T73 and D74. Hydrogen bonds have been identified between -SG and the residues V59 and T73 of Grx(C14S), and the formation of an additional hydrogen bond with Y72 and electrostatic interactions with the side-chains of D74 and K45 are also compatible with the NMR conformational constraints. Comparison of the reduced and oxidized forms of Grx with Grx(C14S)-SG shows that the mixed disulfide more closely resembles the oxidized form of the protein. Functional implications of this observation are discussed. Comparisons are also made with the related proteins bacteriophage T4 glutaredoxin and glutathione S-transferase.
DOI: 10.1006/jmbi.1994.1108
PubMed: 8107093
Affiliations:
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Le document en format XML
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Billeter</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Wuthrich, K" sort="Wuthrich, K" uniqKey="Wuthrich K" first="K" last="Wüthrich">K. Wüthrich</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8107093</idno><idno type="pmid">8107093</idno><idno type="doi">10.1006/jmbi.1994.1108</idno><idno type="wicri:Area/Main/Corpus">001253</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001253</idno><idno type="wicri:Area/Main/Curation">001253</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001253</idno><idno type="wicri:Area/Main/Exploration">001253</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.</title><author><name sortKey="Bushweller, J H" sort="Bushweller, J H" uniqKey="Bushweller J" first="J H" last="Bushweller">J H Bushweller</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich</wicri:regionArea><placeName><settlement type="city">Zurich</settlement><region nuts="3" type="region">Canton de Zurich</region></placeName></affiliation></author><author><name sortKey="Billeter, M" sort="Billeter, M" uniqKey="Billeter M" first="M" last="Billeter">M. Billeter</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Wuthrich, K" sort="Wuthrich, K" uniqKey="Wuthrich K" first="K" last="Wüthrich">K. Wüthrich</name></author></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Bacterial Proteins (MeSH)</term><term>Binding Sites (MeSH)</term><term>Conserved Sequence (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Cysteine (MeSH)</term><term>Disulfides (chemistry)</term><term>Escherichia coli (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Hydrogen Bonding (MeSH)</term><term>Magnetic Resonance Spectroscopy (methods)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Point Mutation (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Folding (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term><term>Solutions (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cystéine (MeSH)</term><term>Disulfures (composition chimique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Liaison hydrogène (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutation ponctuelle (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Pliage des protéines (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (métabolisme)</term><term>Protéines bactériennes (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Solutions (MeSH)</term><term>Spectroscopie par résonance magnétique (méthodes)</term><term>Structure secondaire des protéines (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>Disulfides</term><term>Glutathione</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Bacterial Proteins</term><term>Cysteine</term><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Solutions</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Glutathion</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Magnetic Resonance Spectroscopy</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Glutathion</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Spectroscopie par résonance magnétique</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>Hydrogen Bonding</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Point Mutation</term><term>Protein Conformation</term><term>Protein Folding</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Cystéine</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Mutation ponctuelle</term><term>Oxidoreductases</term><term>Pliage des protéines</term><term>Protéines bactériennes</term><term>Sites de fixation</term><term>Solutions</term><term>Structure secondaire des protéines</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The determination of the nuclear magnetic resonance (NMR) solution structured of the mixed disulfide between the mutant Escherichia coli glutaredoxin Grx(C14S) and glutathione (GSH), Grx(C14S)-SG, is described, the binding site for GSH on Grx(C14S) is located, and the non-bonding interactions between -SG and the protein are characterized. Based on nearly complete sequence-specific NMR assignments, 1010 nuclear Overhauser enhancement upper distance constraints and 116 dihedral angle constraints were obtained as the input for the structure calculations, for which the distance geometry program DIANA was used followed by energy minimization in a waterbath with the AMBER force field in the program OPAL. The -SG moiety was found to be localized on the surface of the protein in a cleft bounded by the amino acid residues Y13, T58, V59, Y72, T73 and D74. Hydrogen bonds have been identified between -SG and the residues V59 and T73 of Grx(C14S), and the formation of an additional hydrogen bond with Y72 and electrostatic interactions with the side-chains of D74 and K45 are also compatible with the NMR conformational constraints. Comparison of the reduced and oxidized forms of Grx with Grx(C14S)-SG shows that the mixed disulfide more closely resembles the oxidized form of the protein. Functional implications of this observation are discussed. Comparisons are also made with the related proteins bacteriophage T4 glutaredoxin and glutathione S-transferase.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8107093</PMID><DateCompleted><Year>1994</Year><Month>03</Month><Day>22</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>235</Volume><Issue>5</Issue><PubDate><Year>1994</Year><Month>Feb</Month><Day>04</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.</ArticleTitle><Pagination><MedlinePgn>1585-97</MedlinePgn></Pagination><Abstract><AbstractText>The determination of the nuclear magnetic resonance (NMR) solution structured of the mixed disulfide between the mutant Escherichia coli glutaredoxin Grx(C14S) and glutathione (GSH), Grx(C14S)-SG, is described, the binding site for GSH on Grx(C14S) is located, and the non-bonding interactions between -SG and the protein are characterized. Based on nearly complete sequence-specific NMR assignments, 1010 nuclear Overhauser enhancement upper distance constraints and 116 dihedral angle constraints were obtained as the input for the structure calculations, for which the distance geometry program DIANA was used followed by energy minimization in a waterbath with the AMBER force field in the program OPAL. The -SG moiety was found to be localized on the surface of the protein in a cleft bounded by the amino acid residues Y13, T58, V59, Y72, T73 and D74. Hydrogen bonds have been identified between -SG and the residues V59 and T73 of Grx(C14S), and the formation of an additional hydrogen bond with Y72 and electrostatic interactions with the side-chains of D74 and K45 are also compatible with the NMR conformational constraints. Comparison of the reduced and oxidized forms of Grx with Grx(C14S)-SG shows that the mixed disulfide more closely resembles the oxidized form of the protein. Functional implications of this observation are discussed. Comparisons are also made with the related proteins bacteriophage T4 glutaredoxin and glutathione S-transferase.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bushweller</LastName><ForeName>J H</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Billeter</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Wüthrich</LastName><ForeName>K</ForeName><Initials>K</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research 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MajorTopicYN="N">Cysteine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</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="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017354" MajorTopicYN="N">Point Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="Y">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="Y">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012996" MajorTopicYN="N">Solutions</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>2</Month><Day>4</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>2</Month><Day>4</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>2</Month><Day>4</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8107093</ArticleId><ArticleId IdType="pii">S0022-2836(84)71108-9</ArticleId><ArticleId IdType="doi">10.1006/jmbi.1994.1108</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Zurich</li></region><settlement><li>Zurich</li></settlement></list><tree><noCountry><name sortKey="Billeter, M" sort="Billeter, M" uniqKey="Billeter M" first="M" last="Billeter">M. Billeter</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Wuthrich, K" sort="Wuthrich, K" uniqKey="Wuthrich K" first="K" last="Wüthrich">K. Wüthrich</name></noCountry><country name="Suisse"><region name="Canton de Zurich"><name sortKey="Bushweller, J H" sort="Bushweller, J H" uniqKey="Bushweller J" first="J H" last="Bushweller">J H Bushweller</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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