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Structural genomics of the severe acute respiratory syndrome coronavirus : Nuclear magnetic resonance structure of the protein nsP7

Identifieur interne : 004D58 ( Main/Exploration ); précédent : 004D57; suivant : 004D59

Structural genomics of the severe acute respiratory syndrome coronavirus : Nuclear magnetic resonance structure of the protein nsP7

Auteurs : Wolfgang Peti [États-Unis] ; Margaret A. Johnson [États-Unis] ; Torsten Herrmann [États-Unis] ; Benjamin W. Neuman [États-Unis] ; Michael J. Buchmeier [États-Unis] ; Mike Nelson [États-Unis] ; Jeremiah Joseph [États-Unis] ; Rebecca Page [États-Unis] ; Raymond C. Stevens [États-Unis] ; Peter Kuhn [États-Unis] ; Kurt Wüthrich [États-Unis]

Source :

RBID : Pascal:05-0455628

Descripteurs français

English descriptors

Abstract

Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (a2 to a4) form a flat up-down-up antiparallel α-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of α-helix and one turn of 310-helix, is packed across the surface of a2 and a3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to a2 and α3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix al. Each of these three areas is thus implicated as a potential site for protein-protein interactions.

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</analytic>
<series>
<title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
<imprint>
<date when="2005">2005</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt>
<title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
</seriesStmt>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Amino Acid Sequence</term>
<term>Coronavirus</term>
<term>Genomics</term>
<term>Microbiology</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Nuclear Magnetic Resonance, Biomolecular</term>
<term>Polyproteins (chemistry)</term>
<term>Protein</term>
<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary (genetics)</term>
<term>RNA Replicase (chemistry)</term>
<term>RNA Replicase (genetics)</term>
<term>RNA Viruses (metabolism)</term>
<term>SARS Virus (chemistry)</term>
<term>Sequence Alignment</term>
<term>Severe acute respiratory syndrome</term>
<term>Viral Proteins (chemistry)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (physiology)</term>
<term>Virology</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Alignement de séquences</term>
<term>Données de séquences moléculaires</term>
<term>Modèles moléculaires</term>
<term>Polyprotéines ()</term>
<term>Protéines virales ()</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (physiologie)</term>
<term>RNA replicase ()</term>
<term>RNA replicase (génétique)</term>
<term>Résonance magnétique nucléaire biomoléculaire</term>
<term>Structure secondaire des protéines</term>
<term>Structure tertiaire des protéines (génétique)</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS ()</term>
<term>Virus à ARN (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Polyproteins</term>
<term>RNA Replicase</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en">
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Protein Structure, Tertiary</term>
<term>RNA Replicase</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Protéines virales</term>
<term>RNA replicase</term>
<term>Structure tertiaire des protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>RNA Viruses</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Virus à ARN</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr">
<term>Protéines virales</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en">
<term>Viral Proteins</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 Structure, Secondary</term>
<term>Sequence Alignment</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr">
<term>Alignement de séquences</term>
<term>Coronavirus</term>
<term>Données de séquences moléculaires</term>
<term>Génomique</term>
<term>Modèles moléculaires</term>
<term>Polyprotéines</term>
<term>Protéine</term>
<term>Microbiologie</term>
<term>Protéines virales</term>
<term>RNA replicase</term>
<term>Résonance magnétique nucléaire biomoléculaire</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Virologie</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
</keywords>
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<front>
<div type="abstract" xml:lang="en">Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices (a2 to a4) form a flat up-down-up antiparallel α-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of α-helix and one turn of 3
<sub>10</sub>
-helix, is packed across the surface of a2 and a3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to a2 and α3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix al. Each of these three areas is thus implicated as a potential site for protein-protein interactions.</div>
</front>
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