NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Identifieur interne : 001283 ( Main/Exploration ); précédent : 001282; suivant : 001284NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.
Auteurs : T H Xia [Suisse] ; J H Bushweller ; P. Sodano ; M. Billeter ; O. Björnberg ; A. Holmgren ; K. WüthrichSource :
- Protein science : a publication of the Protein Society [ 0961-8368 ] ; 1992.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Logiciel (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines (métabolisme), Protéines bactériennes (composition chimique), Similitude de séquences d'acides aminés (MeSH), Spectroscopie par résonance magnétique (méthodes), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Protéines, Protéines bactériennes.
- métabolisme : Escherichia coli, Protéines.
- méthodes : Spectroscopie par résonance magnétique.
- Conformation des protéines, Données de séquences moléculaires, Glutarédoxines, Logiciel, Modèles moléculaires, Oxidoreductases, Oxydoréduction, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Escherichia coli (metabolism), Glutaredoxins (MeSH), Magnetic Resonance Spectroscopy (methods), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Protein Structure, Secondary (MeSH), Proteins (chemistry), Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Software (MeSH).
- MESH :
- chemical , chemistry : Bacterial Proteins, Proteins.
- metabolism : Escherichia coli, Proteins.
- methods : Magnetic Resonance Spectroscopy.
- Amino Acid Sequence, Glutaredoxins, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Protein Conformation, Protein Structure, Secondary, Sequence Homology, Amino Acid, Software.
Abstract
The determination of the NMR structure of oxidized Escherichia coli glutaredoxin in aqueous solution is described, and comparisons of this structure with that of reduced E. coli glutaredoxin and the related proteins E. coli thioredoxin and T4 glutaredoxin are presented. Based on nearly complete sequence-specific 1H-NMR assignments, 804 nuclear Overhauser enhancement distance constraints and 74 dihedral angle constraints were obtained as the input for the structure calculations, for which the distance geometry program DIANA was used followed by simulated annealing with the program X-PLOR. The molecular architecture of oxidized glutaredoxin is made up of three helices and a four-stranded beta-sheet. The three-dimensional structures of oxidized and the recently described reduced glutaredoxin are very similar. Quantitative analysis of the exchange rates of 34 slowly exchanging amide protons from corresponding series of two-dimensional [15N,1H]-correlated spectra of oxidized and reduced glutaredoxin showed close agreement, indicating almost identical hydrogen-bonding patterns. Nonetheless, differences in local dynamics involving residues near the active site and the C-terminal alpha-helix were clearly manifested. Comparison of the structure of E. coli glutaredoxin with those of T4 glutaredoxin and E. coli thioredoxin showed that all three proteins have a similar overall polypeptide fold. An area of the protein surface at the active site containing Arg 8, Cys 11, Pro 12, Tyr 13, Ile 38, Thr 58, Val 59, Pro 60, Gly 71, Tyr 72, and Thr 73 is proposed as a possible site for interaction with other proteins, in particular ribonucleotide reductase. It was found that this area corresponds to previously proposed interaction sites in T4 glutaredoxin and E. coli thioredoxin. The solvent-accessible surface area at the active site of E. coli glutaredoxin showed a general trend to increase upon reduction. Only the sulfhydryl group of Cys 11 is exposed to the solvent, whereas that of Cys 14 is buried and solvent inaccessible.
DOI: 10.1002/pro.5560010302
PubMed: 1304339
PubMed Central: PMC2142208
Affiliations:
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Sodano</name></author><author><name sortKey="Billeter, M" sort="Billeter, M" uniqKey="Billeter M" first="M" last="Billeter">M. Billeter</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="Wuthrich, K" sort="Wuthrich, K" uniqKey="Wuthrich K" first="K" last="Wüthrich">K. Wüthrich</name></author></analytic><series><title level="j">Protein science : a publication of the Protein Society</title><idno type="ISSN">0961-8368</idno><imprint><date when="1992" type="published">1992</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>Escherichia coli (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Magnetic Resonance Spectroscopy (methods)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Software (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Logiciel (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (métabolisme)</term><term>Protéines bactériennes (composition chimique)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Spectroscopie par résonance magnétique (méthodes)</term><term>Structure secondaire des protéines (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" qualifier="composition chimique" xml:lang="fr"><term>Protéines</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Proteins</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>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>Glutaredoxins</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term><term>Sequence Homology, Amino Acid</term><term>Software</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Logiciel</term><term>Modèles moléculaires</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Similitude de séquences d'acides aminés</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The determination of the NMR structure of oxidized Escherichia coli glutaredoxin in aqueous solution is described, and comparisons of this structure with that of reduced E. coli glutaredoxin and the related proteins E. coli thioredoxin and T4 glutaredoxin are presented. Based on nearly complete sequence-specific 1H-NMR assignments, 804 nuclear Overhauser enhancement distance constraints and 74 dihedral angle constraints were obtained as the input for the structure calculations, for which the distance geometry program DIANA was used followed by simulated annealing with the program X-PLOR. The molecular architecture of oxidized glutaredoxin is made up of three helices and a four-stranded beta-sheet. The three-dimensional structures of oxidized and the recently described reduced glutaredoxin are very similar. Quantitative analysis of the exchange rates of 34 slowly exchanging amide protons from corresponding series of two-dimensional [15N,1H]-correlated spectra of oxidized and reduced glutaredoxin showed close agreement, indicating almost identical hydrogen-bonding patterns. Nonetheless, differences in local dynamics involving residues near the active site and the C-terminal alpha-helix were clearly manifested. Comparison of the structure of E. coli glutaredoxin with those of T4 glutaredoxin and E. coli thioredoxin showed that all three proteins have a similar overall polypeptide fold. An area of the protein surface at the active site containing Arg 8, Cys 11, Pro 12, Tyr 13, Ile 38, Thr 58, Val 59, Pro 60, Gly 71, Tyr 72, and Thr 73 is proposed as a possible site for interaction with other proteins, in particular ribonucleotide reductase. It was found that this area corresponds to previously proposed interaction sites in T4 glutaredoxin and E. coli thioredoxin. The solvent-accessible surface area at the active site of E. coli glutaredoxin showed a general trend to increase upon reduction. Only the sulfhydryl group of Cys 11 is exposed to the solvent, whereas that of Cys 14 is buried and solvent inaccessible.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1304339</PMID><DateCompleted><Year>1993</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0961-8368</ISSN><JournalIssue CitedMedium="Print"><Volume>1</Volume><Issue>3</Issue><PubDate><Year>1992</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Protein science : a publication of the Protein Society</Title><ISOAbbreviation>Protein Sci</ISOAbbreviation></Journal><ArticleTitle>NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins.</ArticleTitle><Pagination><MedlinePgn>310-21</MedlinePgn></Pagination><Abstract><AbstractText>The determination of the NMR structure of oxidized Escherichia coli glutaredoxin in aqueous solution is described, and comparisons of this structure with that of reduced E. coli glutaredoxin and the related proteins E. coli thioredoxin and T4 glutaredoxin are presented. Based on nearly complete sequence-specific 1H-NMR assignments, 804 nuclear Overhauser enhancement distance constraints and 74 dihedral angle constraints were obtained as the input for the structure calculations, for which the distance geometry program DIANA was used followed by simulated annealing with the program X-PLOR. The molecular architecture of oxidized glutaredoxin is made up of three helices and a four-stranded beta-sheet. The three-dimensional structures of oxidized and the recently described reduced glutaredoxin are very similar. Quantitative analysis of the exchange rates of 34 slowly exchanging amide protons from corresponding series of two-dimensional [15N,1H]-correlated spectra of oxidized and reduced glutaredoxin showed close agreement, indicating almost identical hydrogen-bonding patterns. Nonetheless, differences in local dynamics involving residues near the active site and the C-terminal alpha-helix were clearly manifested. Comparison of the structure of E. coli glutaredoxin with those of T4 glutaredoxin and E. coli thioredoxin showed that all three proteins have a similar overall polypeptide fold. An area of the protein surface at the active site containing Arg 8, Cys 11, Pro 12, Tyr 13, Ile 38, Thr 58, Val 59, Pro 60, Gly 71, Tyr 72, and Thr 73 is proposed as a possible site for interaction with other proteins, in particular ribonucleotide reductase. It was found that this area corresponds to previously proposed interaction sites in T4 glutaredoxin and E. coli thioredoxin. The solvent-accessible surface area at the active site of E. coli glutaredoxin showed a general trend to increase upon reduction. Only the sulfhydryl group of Cys 11 is exposed to the solvent, whereas that of Cys 14 is buried and solvent inaccessible.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xia</LastName><ForeName>T H</ForeName><Initials>TH</Initials><AffiliationInfo><Affiliation>Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bushweller</LastName><ForeName>J H</ForeName><Initials>JH</Initials></Author><Author ValidYN="Y"><LastName>Sodano</LastName><ForeName>P</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Billeter</LastName><ForeName>M</ForeName><Initials>M</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>Wüthrich</LastName><ForeName>K</ForeName><Initials>K</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><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Protein Sci</MedlineTA><NlmUniqueID>9211750</NlmUniqueID><ISSNLinking>0961-8368</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 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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="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="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="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" 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Billeter</name><name sortKey="Bjornberg, O" sort="Bjornberg, O" uniqKey="Bjornberg O" first="O" last="Björnberg">O. Björnberg</name><name sortKey="Bushweller, J H" sort="Bushweller, J H" uniqKey="Bushweller J" first="J H" last="Bushweller">J H Bushweller</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Sodano, P" sort="Sodano, P" uniqKey="Sodano P" first="P" last="Sodano">P. Sodano</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="Xia, T H" sort="Xia, T H" uniqKey="Xia T" first="T H" last="Xia">T H Xia</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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