SrasV1, PascalFrancis, Corpus, bibRecord, 000475

Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs

Identifieur interne : 000475 ( PascalFrancis/Corpus ); précédent : 000474; suivant : 000476

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 : Pascal:06-0391955

Descripteurs français

Pascal (Inist)
- Coronavirus, Structure cristalline, Protéine, Microbiologie, Virologie, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Crystalline structure, Microbiology, Protein, Severe acute respiratory syndrome, Virology.

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 la and lab, which are cleaved to generate 16 "nonstructural" proteins, nspl to nspl6, 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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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Format Inist (serveur)

NO :	PASCAL 06-0391955 INIST
ET :	Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
AU :	JOSEPH (Jeremiah S.); KUMAR SINGH SAIKATENDU; SUBRAMANIAN (Vanitha); NEUMAN (Benjamin W.); BROOUN (Alexei); GRIFFITH (Mark); MOY (Kin); YADAV (Maneesh K.); VELASQUEZ (Jeffrey); BUCHMEIER (Michael J.); STEVENS (Raymond C.); KUHN (Peter)
AF :	Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 5 aut., 8 aut., 12 aut.); Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 6 aut., 7 aut., 9 aut., 11 aut.); Department of Neumpharmacolagy, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (4 aut., 10 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 16; Pp. 7894-7901; Bibl. 32 ref.
LA :	Anglais
EA :	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 la and lab, which are cleaved to generate 16 "nonstructural" proteins, nspl to nspl6, 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.
CC :	002A05C10
FD :	Coronavirus; Structure cristalline; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère
FG :	Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie
ED :	Coronavirus; Crystalline structure; Protein; Microbiology; Virology; Severe acute respiratory syndrome
EG :	Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease
SD :	Coronavirus; Estructura cristalina; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo
LO :	INIST-13592.354000133387600110
ID :	06-0391955

Links to Exploration step

Pascal:06-0391955

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs</title>
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<series><title level="j" type="main">Journal of virology</title>
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<front><div type="abstract" xml:lang="en">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 la and lab, which are cleaved to generate 16 "nonstructural" proteins, nspl to nspl6, 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.</div>
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<fA08 i1="01" i2="1" l="ENG"><s1>Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs</s1>
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<server><NO>PASCAL 06-0391955 INIST</NO>
<ET>Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs</ET>
<AU>JOSEPH (Jeremiah S.); KUMAR SINGH SAIKATENDU; SUBRAMANIAN (Vanitha); NEUMAN (Benjamin W.); BROOUN (Alexei); GRIFFITH (Mark); MOY (Kin); YADAV (Maneesh K.); VELASQUEZ (Jeffrey); BUCHMEIER (Michael J.); STEVENS (Raymond C.); KUHN (Peter)</AU>
<AF>Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 5 aut., 8 aut., 12 aut.); Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (1 aut., 2 aut., 3 aut., 6 aut., 7 aut., 9 aut., 11 aut.); Department of Neumpharmacolagy, The Scripps Research Institute, 10550 N. Torrey Pines Road/La Jolla, California 92037/Etats-Unis (4 aut., 10 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 16; Pp. 7894-7901; Bibl. 32 ref.</SO>
<LA>Anglais</LA>
<EA>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 la and lab, which are cleaved to generate 16 "nonstructural" proteins, nspl to nspl6, 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.</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Structure cristalline; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère</FD>
<FG>Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie</FG>
<ED>Coronavirus; Crystalline structure; Protein; Microbiology; Virology; Severe acute respiratory syndrome</ED>
<EG>Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease</EG>
<SD>Coronavirus; Estructura cristalina; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo</SD>
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   |wiki=    Sante
   |area=    SrasV1
   |flux=    PascalFrancis
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   |clé=     Pascal:06-0391955
   |texte=   Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
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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

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