SrasV1, Ncbi, Curation, bibRecord, 001180

Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7

Identifieur interne : 001180 ( Ncbi/Curation ); précédent : 001179; suivant : 001181

Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7

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

Source :

Journal of Virology [ 0022-538X ] ; 2005.

RBID : PMC:1235862

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Polyproteins (chemistry), Protein Structure, Secondary, Protein Structure, Tertiary (genetics), RNA Replicase (chemistry), RNA Replicase (genetics), RNA Viruses (metabolism), SARS Virus (chemistry), Sequence Alignment, Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (physiology).
MESH :
- chemical , chemistry : Polyproteins, RNA Replicase, Viral Proteins.
- chemistry : SARS Virus.
- genetics : Protein Structure, Tertiary, RNA Replicase, Viral Proteins.
- metabolism : RNA Viruses.
- chemical , physiology : Viral Proteins.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Secondary, Sequence Alignment.

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 (α2 to α4) 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 α2 and α3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to α2 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 α1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1235862

DOI: 10.1128/JVI.79.20.12905-12913.2005
PubMed: 16188992
PubMed Central: 1235862

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PMC:1235862

Le document en format XML

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<term>Protein Structure, Secondary</term>
<term>Protein Structure, Tertiary (genetics)</term>
<term>RNA Replicase (chemistry)</term>
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<term>Protéines virales ()</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (physiologie)</term>
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<front><div type="abstract" xml:lang="en"><p>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 (α2 to α4) 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 α2 and α3 in the helix sheet, with the α-helical region oriented at a 60° angle relative to α2 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 α1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.</p>
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Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7

Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7

Source :

Descripteurs français

English descriptors

Abstract

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Links to Exploration step

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