NMR structure of oxidized glutaredoxin 3 from Escherichia coli.
Identifieur interne : 001062 ( Main/Exploration ); précédent : 001061; suivant : 001063NMR structure of oxidized glutaredoxin 3 from Escherichia coli.
Auteurs : K. Nordstrand [Suède] ; A. Sandström ; F. Aslund ; A. Holmgren ; G. Otting ; K D BerndtSource :
- Journal of molecular biology [ 0022-2836 ] ; 2000.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Conformation des protéines (effets des médicaments et des substances chimiques), Cystéine (métabolisme), Disulfures (composition chimique), Disulfures (métabolisme), Données de séquences moléculaires (MeSH), Escherichia coli (composition chimique), Glutarédoxines (MeSH), Glutathion (analogues et dérivés), Glutathion (métabolisme), Glutathion (pharmacologie), Liaison aux protéines (MeSH), Liaison hydrogène (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Oxygène (métabolisme), Protéines (composition chimique), Protéines (métabolisme), Réducteurs (métabolisme), Réducteurs (pharmacologie), Résonance magnétique nucléaire biomoléculaire (MeSH), Sites de fixation (MeSH), Solvants (MeSH), Spécificité du substrat (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Thermodynamique (MeSH), Tyrosine (métabolisme).
- MESH :
- analogues et dérivés : Glutathion.
- composition chimique : Disulfures, Escherichia coli, Protéines.
- effets des médicaments et des substances chimiques : Conformation des protéines.
- métabolisme : Cystéine, Disulfures, Glutathion, Oxygène, Protéines, Réducteurs, Tyrosine.
- pharmacologie : Glutathion, Réducteurs.
- Alignement de séquences, Données de séquences moléculaires, Glutarédoxines, Liaison aux protéines, Liaison hydrogène, Modèles moléculaires, Oxidoreductases, Oxydoréduction, Résonance magnétique nucléaire biomoléculaire, Sites de fixation, Solvants, Spécificité du substrat, Séquence conservée, Séquence d'acides aminés, Thermodynamique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Conserved Sequence (MeSH), Cysteine (metabolism), Disulfides (chemistry), Disulfides (metabolism), Escherichia coli (chemistry), Glutaredoxins (MeSH), Glutathione (analogs & derivatives), Glutathione (metabolism), Glutathione (pharmacology), Hydrogen Bonding (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Oxygen (metabolism), Protein Binding (MeSH), Protein Conformation (drug effects), Proteins (chemistry), Proteins (metabolism), Reducing Agents (metabolism), Reducing Agents (pharmacology), Sequence Alignment (MeSH), Solvents (MeSH), Substrate Specificity (MeSH), Thermodynamics (MeSH), Tyrosine (metabolism).
- MESH :
- chemical , analogs & derivatives : Glutathione.
- chemical , chemistry : Disulfides, Proteins.
- chemical , metabolism : Cysteine, Disulfides, Glutathione, Oxygen, Proteins, Reducing Agents, Tyrosine.
- chemistry : Escherichia coli.
- drug effects : Protein Conformation.
- chemical , pharmacology : Glutathione, Reducing Agents.
- Amino Acid Sequence, Binding Sites, Conserved Sequence, Glutaredoxins, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Oxidoreductases, Protein Binding, Sequence Alignment, Solvents, Substrate Specificity, Thermodynamics.
Abstract
A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.
DOI: 10.1006/jmbi.2000.4145
PubMed: 11031118
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Nordstrand</name><affiliation wicri:level="1"><nlm:affiliation>Center for Structural Biochemistry Karolinska Institutet, Huddinge, S-141 57, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Center for Structural Biochemistry Karolinska Institutet, Huddinge, S-141 57</wicri:regionArea><wicri:noRegion>S-141 57</wicri:noRegion></affiliation></author><author><name sortKey="Sandstrom, A" sort="Sandstrom, A" uniqKey="Sandstrom A" first="A" last="Sandström">A. Sandström</name></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</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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Biomolecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxygen (metabolism)</term><term>Protein Binding (MeSH)</term><term>Protein Conformation (drug effects)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term><term>Reducing Agents (metabolism)</term><term>Reducing Agents (pharmacology)</term><term>Sequence Alignment (MeSH)</term><term>Solvents (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Thermodynamics (MeSH)</term><term>Tyrosine (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Conformation des protéines (effets des médicaments et des substances chimiques)</term><term>Cystéine (métabolisme)</term><term>Disulfures (composition chimique)</term><term>Disulfures (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (composition chimique)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion 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scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Liaison aux protéines</term><term>Liaison hydrogène</term><term>Modèles moléculaires</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Sites de fixation</term><term>Solvants</term><term>Spécificité du substrat</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11031118</PMID><DateCompleted><Year>2000</Year><Month>11</Month><Day>30</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>303</Volume><Issue>3</Issue><PubDate><Year>2000</Year><Month>Oct</Month><Day>27</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>NMR structure of oxidized glutaredoxin 3 from Escherichia coli.</ArticleTitle><Pagination><MedlinePgn>423-32</MedlinePgn></Pagination><Abstract><AbstractText>A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides.</AbstractText><CopyrightInformation>Copyright 2000 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nordstrand</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Center for Structural Biochemistry Karolinska Institutet, Huddinge, S-141 57, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sandström</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Aslund</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><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>1FOV</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><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="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>0</RegistryNumber><NameOfSubstance UI="D019163">Reducing Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012997">Solvents</NameOfSubstance></Chemical><Chemical><RegistryNumber>42HK56048U</RegistryNumber><NameOfSubstance UI="D014443">Tyrosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</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="Y">Nuclear Magnetic Resonance, Biomolecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019163" MajorTopicYN="N">Reducing Agents</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012997" MajorTopicYN="N">Solvents</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014443" MajorTopicYN="N">Tyrosine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>10</Month><Day>14</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>2</Month><Day>28</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>10</Month><Day>14</Day><Hour>11</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11031118</ArticleId><ArticleId IdType="doi">10.1006/jmbi.2000.4145</ArticleId><ArticleId IdType="pii">S0022-2836(00)94145-7</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name><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="Sandstrom, A" sort="Sandstrom, A" uniqKey="Sandstrom A" first="A" last="Sandström">A. Sandström</name></noCountry><country name="Suède"><noRegion><name sortKey="Nordstrand, K" sort="Nordstrand, K" uniqKey="Nordstrand K" first="K" last="Nordstrand">K. Nordstrand</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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