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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

Identifieur interne : 000515 ( PascalFrancis/Curation ); précédent : 000514; suivant : 000516

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 [États-Unis] ; KUMAR SINGH SAIKATENDU [États-Unis] ; Vanitha Subramanian [États-Unis] ; Benjamin W. Neuman [États-Unis] ; Alexei Brooun [États-Unis] ; Mark Griffith [États-Unis] ; Kin Moy [États-Unis] ; Maneesh K. Yadav [États-Unis] ; Jeffrey Velasquez [États-Unis] ; Michael J. Buchmeier [États-Unis] ; Raymond C. Stevens [États-Unis] ; Peter Kuhn [États-Unis]

Source :

RBID : Pascal:06-0391955

Descripteurs français

English descriptors

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.
pA  
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A03   1    @0 J. virol.
A05       @2 80
A06       @2 16
A08 01  1  ENG  @1 Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs
A11 01  1    @1 JOSEPH (Jeremiah S.)
A11 02  1    @1 KUMAR SINGH SAIKATENDU
A11 03  1    @1 SUBRAMANIAN (Vanitha)
A11 04  1    @1 NEUMAN (Benjamin W.)
A11 05  1    @1 BROOUN (Alexei)
A11 06  1    @1 GRIFFITH (Mark)
A11 07  1    @1 MOY (Kin)
A11 08  1    @1 YADAV (Maneesh K.)
A11 09  1    @1 VELASQUEZ (Jeffrey)
A11 10  1    @1 BUCHMEIER (Michael J.)
A11 11  1    @1 STEVENS (Raymond C.)
A11 12  1    @1 KUHN (Peter)
A14 01      @1 Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road @2 La Jolla, California 92037 @3 USA @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 5 aut. @Z 8 aut. @Z 12 aut.
A14 02      @1 Department of Molecular Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road @2 La Jolla, California 92037 @3 USA @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 6 aut. @Z 7 aut. @Z 9 aut. @Z 11 aut.
A14 03      @1 Department of Neumpharmacolagy, The Scripps Research Institute, 10550 N. Torrey Pines Road @2 La Jolla, California 92037 @3 USA @Z 4 aut. @Z 10 aut.
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C01 01    ENG  @0 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.
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N21       @1 261
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Pascal:06-0391955

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<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
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