SrasV1, Ncbi, Curation, bibRecord, 001590

Crystal Structure of Nonstructural Protein 10 from the Severe Acute Respiratory Syndrome Coronavirus Reveals a Novel Fold with Two Zinc-Binding Motifs†

Identifieur interne : 001590 ( Ncbi/Curation ); précédent : 001589; suivant : 001591

Crystal Structure of Nonstructural Protein 10 from the Severe Acute Respiratory Syndrome Coronavirus Reveals a Novel Fold with Two Zinc-Binding Motifs†

Auteurs : Jeremiah S. Joseph ; Kumar Singh Saikatendu ; Vanitha Subramanian ; Benjamin W. Neuman ; Alexei Brooun ; Mark Griffith ; Kin Moy ; Maneesh K. Yadav ; Jeffrey Velasquez ; Michael J. Buchmeier ; Raymond C. Stevens ; Peter Kuhn

Source :

Journal of Virology [ 0022-538X ] ; 2006.

RBID : PMC:1563791

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, SARS Virus, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (physiology), Zinc Fingers.
MESH :
- chemical , chemistry : Viral Nonstructural Proteins.
- chemical , physiology : Viral Nonstructural Proteins.
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, SARS Virus, Zinc Fingers.

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins 1a and 1ab, which are cleaved to generate 16 “nonstructural” proteins, nsp1 to nsp16, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 Å as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular β-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn²⁺ ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the “gag-knuckle fold group” of Zn²⁺-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1563791

DOI: 10.1128/JVI.00467-06
PubMed: 16873246
PubMed Central: 1563791

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Le document en format XML

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<front><div type="abstract" xml:lang="en"><p>The severe acute respiratory syndrome coronavirus (SARS-CoV) possesses a large 29.7-kb positive-stranded RNA genome. The first open reading frame encodes replicase polyproteins 1a and 1ab, which are cleaved to generate 16 “nonstructural” proteins, nsp1 to nsp16, involved in viral replication and/or RNA processing. Among these, nsp10 plays a critical role in minus-strand RNA synthesis in a related coronavirus, murine hepatitis virus. Here, we report the crystal structure of SARS-CoV nsp10 at a resolution of 1.8 Å as determined by single-wavelength anomalous dispersion using phases derived from hexatantalum dodecabromide. nsp10 is a single domain protein consisting of a pair of antiparallel N-terminal helices stacked against an irregular β-sheet, a coil-rich C terminus, and two Zn fingers. nsp10 represents a novel fold and is the first structural representative of this family of Zn finger proteins found so far exclusively in coronaviruses. The first Zn finger coordinates a Zn<sup>2+</sup>
 ion in a unique conformation. The second Zn finger, with four cysteines, is a distant member of the “gag-knuckle fold group” of Zn<sup>2+</sup>
-binding domains and appears to maintain the structural integrity of the C-terminal tail. A distinct clustering of basic residues on the protein surface suggests a nucleic acid-binding function. Gel shift assays indicate that in isolation, nsp10 binds single- and double-stranded RNA and DNA with high-micromolar affinity and without obvious sequence specificity. It is possible that nsp10 functions within a larger RNA-binding protein complex. However, its exact role within the replicase complex is still not clear.</p>
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Crystal Structure of Nonstructural Protein 10 from the Severe Acute Respiratory Syndrome Coronavirus Reveals a Novel Fold with Two Zinc-Binding Motifs†

Crystal Structure of Nonstructural Protein 10 from the Severe Acute Respiratory Syndrome Coronavirus Reveals a Novel Fold with Two Zinc-Binding Motifs†

Source :

Descripteurs français

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Abstract

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