Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond.
Identifieur interne : 001108 ( Main/Exploration ); précédent : 001107; suivant : 001109Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond.
Auteurs : K. Nordstrand [Suède] ; F. Aslund ; S. Meunier ; A. Holmgren ; G. Otting ; K D BerndtSource :
- FEBS letters [ 0014-5793 ] ; 1999.
Descripteurs français
- KwdFr :
- Cystéine (composition chimique), Escherichia coli (enzymologie), Glutarédoxines (MeSH), Liaison hydrogène (MeSH), Mutagenèse (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protons (MeSH), Protéines (composition chimique), Protéines bactériennes (composition chimique), Résonance magnétique nucléaire biomoléculaire (MeSH), Sites de fixation (MeSH), Thiols (composition chimique).
- MESH :
- composition chimique : Cystéine, Protéines, Protéines bactériennes, Thiols.
- enzymologie : Escherichia coli.
- Glutarédoxines, Liaison hydrogène, Mutagenèse, Oxidoreductases, Oxydoréduction, Protons, Résonance magnétique nucléaire biomoléculaire, Sites de fixation.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Binding Sites (MeSH), Cysteine (chemistry), Escherichia coli (enzymology), Glutaredoxins (MeSH), Hydrogen Bonding (MeSH), Mutagenesis (MeSH), Nuclear Magnetic Resonance, Biomolecular (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Proteins (chemistry), Protons (MeSH), Sulfhydryl Compounds (chemistry).
- MESH :
- chemical , chemistry : Bacterial Proteins, Cysteine, Proteins, Sulfhydryl Compounds.
- enzymology : Escherichia coli.
- Binding Sites, Glutaredoxins, Hydrogen Bonding, Mutagenesis, Nuclear Magnetic Resonance, Biomolecular, Oxidation-Reduction, Oxidoreductases, Protons.
Abstract
The active site of Escherichia coli glutaredoxin-3 (Grx3) consists of two redox active cysteine residues in the sequence -C11-P-Y-C14-H-. The 1H NMR resonance of the cysteine thiol proton of Cys-14 in reduced Grx3 is observed at 7.6 ppm. The large downfield shift and NOEs observed with this thiol proton resonance suggest the presence of a hydrogen bond with the Cys-11 thiolate, which is shown to have an abnormally low pKa value. A hydrogen bond would also agree with activity data of Grx3 active site mutants. Furthermore, the activity is reduced in a Grx3 H15V mutant, indicating electrostatic contributions to the stabilization of the Cys-11 thiolate.
DOI: 10.1016/s0014-5793(99)00401-9
PubMed: 10338131
Affiliations:
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Aslund</name></author><author><name sortKey="Meunier, S" sort="Meunier, S" uniqKey="Meunier S" first="S" last="Meunier">S. Meunier</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. Otting</name></author><author><name sortKey="Berndt, K D" sort="Berndt, K D" uniqKey="Berndt K" first="K D" last="Berndt">K D Berndt</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10338131</idno><idno type="pmid">10338131</idno><idno type="doi">10.1016/s0014-5793(99)00401-9</idno><idno type="wicri:Area/Main/Corpus">001108</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001108</idno><idno type="wicri:Area/Main/Curation">001108</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001108</idno><idno type="wicri:Area/Main/Exploration">001108</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond.</title><author><name sortKey="Nordstrand, K" sort="Nordstrand, K" uniqKey="Nordstrand K" first="K" last="Nordstrand">K. Nordstrand</name><affiliation wicri:level="3"><nlm:affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name></author><author><name sortKey="Meunier, S" sort="Meunier, S" uniqKey="Meunier S" first="S" last="Meunier">S. Meunier</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. Otting</name></author><author><name sortKey="Berndt, K D" sort="Berndt, K D" uniqKey="Berndt K" first="K D" last="Berndt">K D Berndt</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Binding Sites (MeSH)</term><term>Cysteine (chemistry)</term><term>Escherichia coli (enzymology)</term><term>Glutaredoxins (MeSH)</term><term>Hydrogen Bonding (MeSH)</term><term>Mutagenesis (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (chemistry)</term><term>Protons (MeSH)</term><term>Sulfhydryl Compounds (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cystéine (composition chimique)</term><term>Escherichia coli (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Liaison hydrogène (MeSH)</term><term>Mutagenèse (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protons (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines bactériennes (composition chimique)</term><term>Résonance magnétique nucléaire biomoléculaire (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Thiols (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Cysteine</term><term>Proteins</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Protéines</term><term>Protéines bactériennes</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Glutaredoxins</term><term>Hydrogen Bonding</term><term>Mutagenesis</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Protons</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Liaison hydrogène</term><term>Mutagenèse</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Protons</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The active site of Escherichia coli glutaredoxin-3 (Grx3) consists of two redox active cysteine residues in the sequence -C11-P-Y-C14-H-. The 1H NMR resonance of the cysteine thiol proton of Cys-14 in reduced Grx3 is observed at 7.6 ppm. The large downfield shift and NOEs observed with this thiol proton resonance suggest the presence of a hydrogen bond with the Cys-11 thiolate, which is shown to have an abnormally low pKa value. A hydrogen bond would also agree with activity data of Grx3 active site mutants. Furthermore, the activity is reduced in a Grx3 H15V mutant, indicating electrostatic contributions to the stabilization of the Cys-11 thiolate.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10338131</PMID><DateCompleted><Year>1999</Year><Month>06</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>449</Volume><Issue>2-3</Issue><PubDate><Year>1999</Year><Month>Apr</Month><Day>23</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond.</ArticleTitle><Pagination><MedlinePgn>196-200</MedlinePgn></Pagination><Abstract><AbstractText>The active site of Escherichia coli glutaredoxin-3 (Grx3) consists of two redox active cysteine residues in the sequence -C11-P-Y-C14-H-. The 1H NMR resonance of the cysteine thiol proton of Cys-14 in reduced Grx3 is observed at 7.6 ppm. The large downfield shift and NOEs observed with this thiol proton resonance suggest the presence of a hydrogen bond with the Cys-11 thiolate, which is shown to have an abnormally low pKa value. A hydrogen bond would also agree with activity data of Grx3 active site mutants. 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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="Meunier, S" sort="Meunier, S" uniqKey="Meunier S" first="S" last="Meunier">S. Meunier</name><name sortKey="Otting, G" sort="Otting, G" uniqKey="Otting G" first="G" last="Otting">G. Otting</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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