SrasV1, PascalFrancis, Curation, bibRecord, 000516

Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10

Identifieur interne : 000516 ( PascalFrancis/Curation ); précédent : 000515; suivant : 000517

Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10

Auteurs : DAN SU [République populaire de Chine] ; ZHIYONG LOU [République populaire de Chine] ; FEI SUN [République populaire de Chine] ; YUJIA ZHAI [République populaire de Chine] ; HAITAO YANG [République populaire de Chine] ; RONGGUANG ZHANG [République populaire de Chine, États-Unis] ; Andrzej Joachimiak [États-Unis] ; Xuejun C. Zhang [République populaire de Chine, États-Unis] ; Mark Bartlam [République populaire de Chine] ; ZIHE RAO [République populaire de Chine]

Source :

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

RBID : Pascal:06-0391956

Descripteurs français

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

English descriptors

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

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nspl to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-Å resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)₂-C-(X)₅-H-(X)₆-C and C-(X)₂-C-(X)₇-C-(X)-C. The nsp10 crystal structure is the first of a new class of zinc finger protein three-dimensional structures to be revealed experimentally. The zinc finger sequence motifs are conserved among all three coronavirus antigenic groups, implicating an essential function for nsp10 in all coronaviruses. Based on the structure, we propose that nsp10 is a transcription factor for coronavirus replication/transcription.

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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10</title>
<author><name sortKey="Dan Su" sort="Dan Su" uniqKey="Dan Su" last="Dan Su">DAN SU</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
<s2>Beijing 100084</s2>
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<affiliation wicri:level="1"><inist:fA14 i1="02"><s1>National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences</s1>
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<author><name sortKey="Zhiyong Lou" sort="Zhiyong Lou" uniqKey="Zhiyong Lou" last="Zhiyong Lou">ZHIYONG LOU</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
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<author><name sortKey="Joachimiak, Andrzej" sort="Joachimiak, Andrzej" uniqKey="Joachimiak A" first="Andrzej" last="Joachimiak">Andrzej Joachimiak</name>
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<author><name sortKey="Bartlam, Mark" sort="Bartlam, Mark" uniqKey="Bartlam M" first="Mark" last="Bartlam">Mark Bartlam</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
<s2>Beijing 100084</s2>
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<author><name sortKey="Zihe Rao" sort="Zihe Rao" uniqKey="Zihe Rao" last="Zihe Rao">ZIHE RAO</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
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<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="2006">2006</date>
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<seriesStmt><title level="j" type="main">Journal of virology</title>
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<idno type="ISSN">0022-538X</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term>
<term>Microbiology</term>
<term>Protein</term>
<term>Severe acute respiratory syndrome</term>
<term>Virology</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term>
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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nspl to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-Å resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)<sub>2</sub>
-C-(X)<sub>5</sub>
-H-(X)<sub>6</sub>
-C and C-(X)<sub>2</sub>
-C-(X)<sub>7</sub>
-C-(X)-C. The nsp10 crystal structure is the first of a new class of zinc finger protein three-dimensional structures to be revealed experimentally. The zinc finger sequence motifs are conserved among all three coronavirus antigenic groups, implicating an essential function for nsp10 in all coronaviruses. Based on the structure, we propose that nsp10 is a transcription factor for coronavirus replication/transcription.</div>
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<fA08 i1="01" i2="1" l="ENG"><s1>Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10</s1>
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<fA11 i1="01" i2="1"><s1>DAN SU</s1>
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<fA11 i1="02" i2="1"><s1>ZHIYONG LOU</s1>
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<fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
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<fC01 i1="01" l="ENG"><s0>The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nspl to nsp16 have been implicated by genetic analysis in the assembly of a functional replication/transcription complex. We report the crystal structure of nsp10 from SARS-CoV at 2.1-Å resolution. The nsp10 structure has a novel fold, and 12 identical subunits assemble to form a unique spherical dodecameric architecture. Two zinc fingers have been identified from the nsp10 monomer structure with the sequence motifs C-(X)<sub>2</sub>
-C-(X)<sub>5</sub>
-H-(X)<sub>6</sub>
-C and C-(X)<sub>2</sub>
-C-(X)<sub>7</sub>
-C-(X)-C. The nsp10 crystal structure is the first of a new class of zinc finger protein three-dimensional structures to be revealed experimentally. The zinc finger sequence motifs are conserved among all three coronavirus antigenic groups, implicating an essential function for nsp10 in all coronaviruses. Based on the structure, we propose that nsp10 is a transcription factor for coronavirus replication/transcription.</s0>
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Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10

Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10

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