Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
Identifieur interne : 003779 ( Main/Merge ); précédent : 003778; suivant : 003780Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
Auteurs : Marcius S. Almeida [États-Unis] ; Margaret A. Johnson ; Torsten Herrmann ; Michael Geralt ; Kurt WüthrichSource :
- Journal of virology [ 0022-538X ] ; 2007.
Descripteurs français
- KwdFr :
- Données de séquences moléculaires, Fragments peptidiques (), Fragments peptidiques (génétique), Fragments peptidiques (métabolisme), Modèles moléculaires, Pliage des protéines, Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), RNA replicase (), RNA replicase (génétique), RNA replicase (métabolisme), Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Virus du SRAS (enzymologie), Virus du SRAS (génétique).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : Fragments peptidiques, Protéines recombinantes, Protéines virales non structurales, RNA replicase, Virus du SRAS.
- métabolisme : Fragments peptidiques, Protéines recombinantes, Protéines virales non structurales, RNA replicase.
- Données de séquences moléculaires, Fragments peptidiques, Modèles moléculaires, Pliage des protéines, Protéines recombinantes, Protéines virales non structurales, RNA replicase, Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments (chemistry), Peptide Fragments (genetics), Peptide Fragments (metabolism), Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (enzymology), SARS Virus (genetics), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Peptide Fragments, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , genetics : Peptide Fragments, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins.
- chemical , metabolism : Peptide Fragments, RNA Replicase, Recombinant Proteins, Viral Nonstructural Proteins.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary.
Abstract
The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel alpha/beta-fold formed by a mixed parallel/antiparallel six-stranded beta-barrel, an alpha-helix covering one opening of the barrel, and a 3(10)-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA.
DOI: 10.1128/JVI.01939-06
PubMed: 17202208
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pubmed:17202208Le document en format XML
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Johnson</name></author><author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</name></author><author><name sortKey="Geralt, Michael" sort="Geralt, Michael" uniqKey="Geralt M" first="Michael" last="Geralt">Michael Geralt</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="2007">2007</date><idno type="RBID">pubmed:17202208</idno><idno type="pmid">17202208</idno><idno type="doi">10.1128/JVI.01939-06</idno><idno type="wicri:Area/PubMed/Corpus">001F31</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001F31</idno><idno type="wicri:Area/PubMed/Curation">001F31</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001F31</idno><idno type="wicri:Area/PubMed/Checkpoint">001D51</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001D51</idno><idno type="wicri:Area/Ncbi/Merge">001827</idno><idno type="wicri:Area/Ncbi/Curation">001827</idno><idno type="wicri:Area/Ncbi/Checkpoint">001827</idno><idno type="wicri:doubleKey">0022-538X:2007:Almeida M:novel:beta:barrel</idno><idno type="wicri:Area/Main/Merge">003779</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.</title><author><name sortKey="Almeida, Marcius S" sort="Almeida, Marcius S" uniqKey="Almeida M" first="Marcius S" last="Almeida">Marcius S. Almeida</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Biology, MB-44, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Molecular Biology, MB-44, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Johnson, Margaret A" sort="Johnson, Margaret A" uniqKey="Johnson M" first="Margaret A" last="Johnson">Margaret A. Johnson</name></author><author><name sortKey="Herrmann, Torsten" sort="Herrmann, Torsten" uniqKey="Herrmann T" first="Torsten" last="Herrmann">Torsten Herrmann</name></author><author><name sortKey="Geralt, Michael" sort="Geralt, Michael" uniqKey="Geralt M" first="Michael" last="Geralt">Michael Geralt</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 virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (genetics)</term><term>Peptide Fragments (metabolism)</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>RNA Replicase (chemistry)</term><term>RNA Replicase (genetics)</term><term>RNA Replicase (metabolism)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (enzymology)</term><term>SARS Virus (genetics)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (génétique)</term><term>Fragments peptidiques (métabolisme)</term><term>Modèles moléculaires</term><term>Pliage des protéines</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines virales non structurales ()</term><term>Protéines virales non structurales (génétique)</term><term>Protéines virales non structurales (métabolisme)</term><term>RNA replicase ()</term><term>RNA replicase (génétique)</term><term>RNA replicase (métabolisme)</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (enzymologie)</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Fragments</term><term>RNA Replicase</term><term>Recombinant Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptide Fragments</term><term>RNA Replicase</term><term>Recombinant Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Fragments</term><term>RNA Replicase</term><term>Recombinant Proteins</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Fragments peptidiques</term><term>Protéines recombinantes</term><term>Protéines virales non structurales</term><term>RNA replicase</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fragments peptidiques</term><term>Protéines recombinantes</term><term>Protéines virales non structurales</term><term>RNA replicase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Nuclear Magnetic Resonance, Biomolecular</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Fragments peptidiques</term><term>Modèles moléculaires</term><term>Pliage des protéines</term><term>Protéines recombinantes</term><term>Protéines virales non structurales</term><term>RNA replicase</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel alpha/beta-fold formed by a mixed parallel/antiparallel six-stranded beta-barrel, an alpha-helix covering one opening of the barrel, and a 3(10)-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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