Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.
Identifieur interne : 001295 ( Main/Exploration ); précédent : 001294; suivant : 001296Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.
Auteurs : P. Sodano [Suisse] ; T H Xia ; J H Bushweller ; O. Björnberg ; A. Holmgren ; M. Billeter ; K. WüthrichSource :
- Journal of molecular biology [ 0022-2836 ] ; 1991.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (composition chimique), Glutarédoxines (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines bactériennes (composition chimique), Spectroscopie par résonance magnétique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Escherichia coli (chemistry), Glutaredoxins (MeSH), Magnetic Resonance Spectroscopy (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Protein Conformation (MeSH), Proteins (chemistry).
- MESH :
- chemical , chemistry : Bacterial Proteins, Proteins.
- chemistry : Escherichia coli.
- Amino Acid Sequence, Glutaredoxins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Protein Conformation.
Abstract
The determination of the nuclear magnetic resonance structure of reduced E. coli glutaredoxin in aqueous solution is described. Based on nearly complete, sequence-specific resonance assignments, 813 nuclear Overhauser effect distance constraints and 191 dihedral angle constraints were employed 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 reduced glutaredoxin is made up of three helices and four-stranded beta-sheet. The first strand of the beta-sheet (residues 2 to 7) runs parallel to the second strand (32 to 37) and antiparallel to the third strand (61 to 64), and the sheet is extended in an antiparallel fashion with a fourth strand (67 to 69). The first helix with residues 13 to 28 and the last helix (71 to 83) run parallel to each other on one side of the beta-sheet, with their direction opposite to that of the two parallel beta-strands, and the helix formed by residues 44 to 53 fills space available due to the twist of the beta-sheet and the reduced length of the last two beta-strands. The active site Cys11-Pro-Tyr-Cys14 is located after the first beta-strand and occupies the latter part of the loop connecting this strand with the first helix.
DOI: 10.1016/0022-2836(91)90935-y
PubMed: 1942053
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="Xia, T H" sort="Xia, T H" uniqKey="Xia T" first="T H" last="Xia">T H Xia</name></author><author><name sortKey="Bushweller, J H" sort="Bushweller, J H" uniqKey="Bushweller J" first="J H" last="Bushweller">J H Bushweller</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="Billeter, M" sort="Billeter, M" uniqKey="Billeter M" first="M" last="Billeter">M. Billeter</name></author><author><name sortKey="Wuthrich, K" sort="Wuthrich, K" uniqKey="Wuthrich K" first="K" last="Wüthrich">K. 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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="Xia, T H" sort="Xia, T H" uniqKey="Xia T" first="T H" last="Xia">T H Xia</name></author><author><name sortKey="Bushweller, J H" sort="Bushweller, J H" uniqKey="Bushweller J" first="J H" last="Bushweller">J H Bushweller</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="Billeter, M" sort="Billeter, M" uniqKey="Billeter M" first="M" last="Billeter">M. Billeter</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="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>Escherichia coli (chemistry)</term><term>Glutaredoxins (MeSH)</term><term>Magnetic Resonance Spectroscopy (MeSH)</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>Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (composition chimique)</term><term>Glutarédoxines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines bactériennes (composition chimique)</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" qualifier="chemistry" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="composition chimique" 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>Models, Molecular</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>Modèles moléculaires</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">The determination of the nuclear magnetic resonance structure of reduced E. coli glutaredoxin in aqueous solution is described. Based on nearly complete, sequence-specific resonance assignments, 813 nuclear Overhauser effect distance constraints and 191 dihedral angle constraints were employed 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 reduced glutaredoxin is made up of three helices and four-stranded beta-sheet. The first strand of the beta-sheet (residues 2 to 7) runs parallel to the second strand (32 to 37) and antiparallel to the third strand (61 to 64), and the sheet is extended in an antiparallel fashion with a fourth strand (67 to 69). The first helix with residues 13 to 28 and the last helix (71 to 83) run parallel to each other on one side of the beta-sheet, with their direction opposite to that of the two parallel beta-strands, and the helix formed by residues 44 to 53 fills space available due to the twist of the beta-sheet and the reduced length of the last two beta-strands. The active site Cys11-Pro-Tyr-Cys14 is located after the first beta-strand and occupies the latter part of the loop connecting this strand with the first helix.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1942053</PMID><DateCompleted><Year>1991</Year><Month>12</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>07</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>221</Volume><Issue>4</Issue><PubDate><Year>1991</Year><Month>Oct</Month><Day>20</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>1311-24</MedlinePgn></Pagination><Abstract><AbstractText>The determination of the nuclear magnetic resonance structure of reduced E. coli glutaredoxin in aqueous solution is described. Based on nearly complete, sequence-specific resonance assignments, 813 nuclear Overhauser effect distance constraints and 191 dihedral angle constraints were employed 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 reduced glutaredoxin is made up of three helices and four-stranded beta-sheet. The first strand of the beta-sheet (residues 2 to 7) runs parallel to the second strand (32 to 37) and antiparallel to the third strand (61 to 64), and the sheet is extended in an antiparallel fashion with a fourth strand (67 to 69). The first helix with residues 13 to 28 and the last helix (71 to 83) run parallel to each other on one side of the beta-sheet, with their direction opposite to that of the two parallel beta-strands, and the helix formed by residues 44 to 53 fills space available due to the twist of the beta-sheet and the reduced length of the last two beta-strands. The active site Cys11-Pro-Tyr-Cys14 is located after the first beta-strand and occupies the latter part of the loop connecting this strand with the first helix.</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>Xia</LastName><ForeName>T H</ForeName><Initials>TH</Initials></Author><Author ValidYN="Y"><LastName>Bushweller</LastName><ForeName>J H</ForeName><Initials>JH</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>Billeter</LastName><ForeName>M</ForeName><Initials>M</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 Support, U.S. Gov't, P.H.S.</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="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="N">chemistry</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="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</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="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></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>10</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>10</Month><Day>20</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>10</Month><Day>20</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1942053</ArticleId><ArticleId IdType="pii">0022-2836(91)90935-Y</ArticleId><ArticleId IdType="doi">10.1016/0022-2836(91)90935-y</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="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="Wuthrich, K" sort="Wuthrich, K" uniqKey="Wuthrich K" first="K" last="Wüthrich">K. Wüthrich</name><name sortKey="Xia, T H" sort="Xia, T H" uniqKey="Xia T" first="T H" last="Xia">T H Xia</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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