SrasV1, PubMed, Corpus, bibRecord, 001647

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

Identifieur interne : 001647 ( PubMed/Corpus ); précédent : 001646; suivant : 001648

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

Auteurs : Margaret A. Johnson ; Kristaps Jaudzems ; Kurt Wüthrich

Source :

Journal of molecular biology [ 1089-8638 ] ; 2010.

RBID : pubmed:20709084

English descriptors

KwdEn :
- Hydrogen-Ion Concentration, Kinetics, Magnetic Resonance Spectroscopy (methods), Protein Conformation, Protein Structure, Secondary, SARS Virus (chemistry), Solutions, Viral Nonstructural Proteins (chemistry).
MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical : Solutions.
- chemistry : SARS Virus.
- methods : Magnetic Resonance Spectroscopy.
- Hydrogen-Ion Concentration, Kinetics, Protein Conformation, Protein Structure, Secondary.

Abstract

The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.

DOI: 10.1016/j.jmb.2010.07.043
PubMed: 20709084

Links to Exploration step

pubmed:20709084

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.</title>
<author><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name>
<affiliation><nlm:affiliation>Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Jaudzems, Kristaps" sort="Jaudzems, Kristaps" uniqKey="Jaudzems K" first="Kristaps" last="Jaudzems">Kristaps Jaudzems</name>
</author>
<author><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2010">2010</date>
<idno type="RBID">pubmed:20709084</idno>
<idno type="pmid">20709084</idno>
<idno type="doi">10.1016/j.jmb.2010.07.043</idno>
<idno type="wicri:Area/PubMed/Corpus">001647</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001647</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.</title>
<author><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name>
<affiliation><nlm:affiliation>Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Jaudzems, Kristaps" sort="Jaudzems, Kristaps" uniqKey="Jaudzems K" first="Kristaps" last="Jaudzems">Kristaps Jaudzems</name>
</author>
<author><name sortKey="Wuthrich, Kurt" sort="Wuthrich, Kurt" uniqKey="Wuthrich K" first="Kurt" last="Wüthrich">Kurt Wüthrich</name>
</author>
</analytic>
<series><title level="j">Journal of molecular biology</title>
<idno type="eISSN">1089-8638</idno>
<imprint><date when="2010" type="published">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Magnetic Resonance Spectroscopy (methods)</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
<term>SARS Virus (chemistry)</term>
<term>Solutions</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Nonstructural Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Solutions</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Magnetic Resonance Spectroscopy</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Protein Conformation</term>
<term>Protein Structure, Secondary</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20709084</PMID>
<DateCompleted><Year>2010</Year>
<Month>11</Month>
<Day>02</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>08</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1089-8638</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>402</Volume>
<Issue>4</Issue>
<PubDate><Year>2010</Year>
<Month>Oct</Month>
<Day>01</Day>
</PubDate>
</JournalIssue>
<Title>Journal of molecular biology</Title>
<ISOAbbreviation>J. Mol. Biol.</ISOAbbreviation>
</Journal>
<ArticleTitle>NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.</ArticleTitle>
<Pagination><MedlinePgn>619-28</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.jmb.2010.07.043</ELocationID>
<Abstract><AbstractText>The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.</AbstractText>
<CopyrightInformation>Copyright © 2010 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Margaret A</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jaudzems</LastName>
<ForeName>Kristaps</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Wüthrich</LastName>
<ForeName>Kurt</ForeName>
<Initials>K</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName>
<AccessionNumberList><AccessionNumber>2KYS</AccessionNumber>
</AccessionNumberList>
</DataBank>
</DataBankList>
<GrantList CompleteYN="Y"><Grant><GrantID>U54 GM074898</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>U54-GM074898</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2010</Year>
<Month>08</Month>
<Day>13</Day>
</ArticleDate>
</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="D012996">Solutions</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName>
<QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012996" MajorTopicYN="N">Solutions</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year>
<Month>06</Month>
<Day>11</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2010</Year>
<Month>07</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2010</Year>
<Month>07</Month>
<Day>23</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2010</Year>
<Month>8</Month>
<Day>17</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2010</Year>
<Month>8</Month>
<Day>17</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2010</Year>
<Month>11</Month>
<Day>3</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">20709084</ArticleId>
<ArticleId IdType="pii">S0022-2836(10)00819-3</ArticleId>
<ArticleId IdType="doi">10.1016/j.jmb.2010.07.043</ArticleId>
<ArticleId IdType="pmc">PMC3081601</ArticleId>
<ArticleId IdType="mid">NIHMS234447</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Adv Exp Med Biol. 2001;494:291-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11774483</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Microbiol. 2009 Jun;7(6):439-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19430490</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 2002 May;23(1):23-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12061715</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 2002 Nov;24(3):171-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12522306</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Sep;78(18):9977-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15331731</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2004 Oct 8;323(1):264-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15351731</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Nov;78(21):11551-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15479796</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biopolymers. 1983 Dec;22(12):2577-637</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6667333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1993 Sep 5;233(1):123-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8377180</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 1993 Sep;17(1):75-86</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8234246</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Nov 10;270(45):26962-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7592943</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Trends Biochem Sci. 1995 Nov;20(11):478-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8578593</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 1995 Sep;6(2):135-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8589602</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Graph. 1996 Feb;14(1):51-5, 29-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8744573</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1996 Sep;134(6):1387-99</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8830769</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 1996 Sep;8(2):136-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8914272</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1997 Oct 17;273(1):283-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9367762</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Sci. 1998 Jan;7(1):21-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9514257</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Jan;73(1):177-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9847320</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Oct;73(10):7952-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10482542</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virol J. 2005;2:69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16115318</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Oct;79(20):12905-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16188992</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2005 Nov;12(11):980-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16228002</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 2006 May 1;63(2):336-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16372350</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Apr;74(7):3379-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10708455</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Res. 2006 Apr;117(1):17-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16503362</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Virus Res. 2006;66:193-292</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16877062</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2006 Oct 18;25(20):4933-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17024178</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2007 May 10;361(2):304-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17210170</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2007 Oct;81(19):10280-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17634238</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Jun;82(11):5279-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18367524</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biomol NMR. 2008 Sep;42(1):23-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18709333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2002 May 24;319(1):209-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12051947</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001647 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 001647 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    PubMed
   |étape=   Corpus
   |type=    RBID
   |clé=     pubmed:20709084
   |texte=   NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i   -Sk "pubmed:20709084" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

	Serveur d'exploration SRAS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration SRAS

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki