Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form.
Identifieur interne : 001299 ( Main/Exploration ); précédent : 001298; suivant : 001300Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form.
Auteurs : P. Sodano [Suisse] ; K V Chary ; O. Björnberg ; A. Holmgren ; B. Kren ; J A Fuchs ; K. WüthrichSource :
- European journal of biochemistry [ 0014-2956 ] ; 1991.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Glutarédoxines (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines (génétique), Protéines bactériennes (composition chimique), Protéines bactériennes (génétique), Spectroscopie par résonance magnétique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Protéines, Protéines bactériennes.
- génétique : Escherichia coli, Protéines, Protéines bactériennes.
- Conformation des protéines, Données de séquences moléculaires, Glutarédoxines, Oxidoreductases, Oxydoréduction, Spectroscopie par résonance magnétique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Escherichia coli (genetics), Glutaredoxins (MeSH), Magnetic Resonance Spectroscopy (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Proteins (chemistry), Proteins (genetics).
- MESH :
- chemical , chemistry : Bacterial Proteins, Proteins.
- chemical , genetics : Bacterial Proteins, Proteins.
- genetics : Escherichia coli.
- Amino Acid Sequence, Glutaredoxins, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Protein Conformation.
Abstract
Escherichia coli glutaredoxin (85 amino acid residues, Mr = 9100), the glutathione-dependent hydrogen donor for ribonucleotide reductase, was purified from an inducible lambda PL, expression system both with a natural isotope content and with uniform 15N labelling. This material was used for obtaining sequence-specific 1H magnetic resonance assignments and the identification of regular secondary structures in the oxidized form of the protein, which contains the redox-active disulfide Cys11-Pro-Tyr-Cys14. Oxidized glutaredoxin contains a four-stranded beta-sheet, with the peripheral strand 32-37 arranged parallel to the strand 2-7, which further combines with the two additional strands 61-64 and 67-69 in an antiparallel fashion. The protein further contains three helices extending approximately from residues 13-28, 45-54 and 72-84.
DOI: 10.1111/j.1432-1033.1991.tb16194.x
PubMed: 1889405
Affiliations:
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Sodano</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Molekularbiologie und Biophysik, Eidgenössiche Technische Hochschule-Hönggerberg, Zürich, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institut für Molekularbiologie und Biophysik, Eidgenössiche 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="Chary, K V" sort="Chary, K V" uniqKey="Chary K" first="K V" last="Chary">K V Chary</name></author><author><name sortKey="Bjornberg, O" sort="Bjornberg, O" uniqKey="Bjornberg O" first="O" last="Björnberg">O. Björnberg</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Kren, B" sort="Kren, B" uniqKey="Kren B" first="B" last="Kren">B. 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Sequence-specific assignments and secondary structure determination of the oxidized form.</title><author><name sortKey="Sodano, P" sort="Sodano, P" uniqKey="Sodano P" first="P" last="Sodano">P. Sodano</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Molekularbiologie und Biophysik, Eidgenössiche Technische Hochschule-Hönggerberg, Zürich, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Institut für Molekularbiologie und Biophysik, Eidgenössiche 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="Chary, K V" sort="Chary, K V" uniqKey="Chary K" first="K V" last="Chary">K V Chary</name></author><author><name sortKey="Bjornberg, O" sort="Bjornberg, O" uniqKey="Bjornberg O" first="O" last="Björnberg">O. Björnberg</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Kren, B" sort="Kren, B" uniqKey="Kren B" first="B" last="Kren">B. Kren</name></author><author><name sortKey="Fuchs, J A" sort="Fuchs, J A" uniqKey="Fuchs J" first="J A" last="Fuchs">J A Fuchs</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">European journal of biochemistry</title><idno type="ISSN">0014-2956</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (genetics)</term><term>Escherichia coli (genetics)</term><term>Glutaredoxins (MeSH)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (génétique)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (génétique)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (génétique)</term><term>Spectroscopie par résonance magnétique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Glutaredoxins</term><term>Magnetic Resonance Spectroscopy</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Protein Conformation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Spectroscopie par résonance magnétique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Escherichia coli glutaredoxin (85 amino acid residues, Mr = 9100), the glutathione-dependent hydrogen donor for ribonucleotide reductase, was purified from an inducible lambda PL, expression system both with a natural isotope content and with uniform 15N labelling. This material was used for obtaining sequence-specific 1H magnetic resonance assignments and the identification of regular secondary structures in the oxidized form of the protein, which contains the redox-active disulfide Cys11-Pro-Tyr-Cys14. Oxidized glutaredoxin contains a four-stranded beta-sheet, with the peripheral strand 32-37 arranged parallel to the strand 2-7, which further combines with the two additional strands 61-64 and 67-69 in an antiparallel fashion. The protein further contains three helices extending approximately from residues 13-28, 45-54 and 72-84.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1889405</PMID><DateCompleted><Year>1991</Year><Month>10</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-2956</ISSN><JournalIssue CitedMedium="Print"><Volume>200</Volume><Issue>2</Issue><PubDate><Year>1991</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>European journal of biochemistry</Title><ISOAbbreviation>Eur J Biochem</ISOAbbreviation></Journal><ArticleTitle>Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin. Sequence-specific assignments and secondary structure determination of the oxidized form.</ArticleTitle><Pagination><MedlinePgn>369-77</MedlinePgn></Pagination><Abstract><AbstractText>Escherichia coli glutaredoxin (85 amino acid residues, Mr = 9100), the glutathione-dependent hydrogen donor for ribonucleotide reductase, was purified from an inducible lambda PL, expression system both with a natural isotope content and with uniform 15N labelling. This material was used for obtaining sequence-specific 1H magnetic resonance assignments and the identification of regular secondary structures in the oxidized form of the protein, which contains the redox-active disulfide Cys11-Pro-Tyr-Cys14. Oxidized glutaredoxin contains a four-stranded beta-sheet, with the peripheral strand 32-37 arranged parallel to the strand 2-7, which further combines with the two additional strands 61-64 and 67-69 in an antiparallel fashion. The protein further contains three helices extending approximately from residues 13-28, 45-54 and 72-84.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sodano</LastName><ForeName>P</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institut für Molekularbiologie und Biophysik, Eidgenössiche Technische Hochschule-Hönggerberg, Zürich, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chary</LastName><ForeName>K V</ForeName><Initials>KV</Initials></Author><Author ValidYN="Y"><LastName>Björnberg</LastName><ForeName>O</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Kren</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Fuchs</LastName><ForeName>J A</ForeName><Initials>JA</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="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Eur J Biochem</MedlineTA><NlmUniqueID>0107600</NlmUniqueID><ISSNLinking>0014-2956</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</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="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="Y">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</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="N">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></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1889405</ArticleId><ArticleId IdType="doi">10.1111/j.1432-1033.1991.tb16194.x</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="Bjornberg, O" sort="Bjornberg, O" uniqKey="Bjornberg O" first="O" last="Björnberg">O. Björnberg</name><name sortKey="Chary, K V" sort="Chary, K V" uniqKey="Chary K" first="K V" last="Chary">K V Chary</name><name sortKey="Fuchs, J A" sort="Fuchs, J A" uniqKey="Fuchs J" first="J A" last="Fuchs">J A Fuchs</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Kren, B" sort="Kren, B" uniqKey="Kren B" first="B" last="Kren">B. Kren</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="Sodano, P" sort="Sodano, P" uniqKey="Sodano P" first="P" last="Sodano">P. Sodano</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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