Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10
Identifieur interne : 000474 ( PascalFrancis/Corpus ); précédent : 000473; suivant : 000475Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10
Auteurs : DAN SU ; ZHIYONG LOU ; FEI SUN ; YUJIA ZHAI ; HAITAO YANG ; RONGGUANG ZHANG ; Andrzej Joachimiak ; Xuejun C. Zhang ; Mark Bartlam ; ZIHE RAOSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- Pascal (Inist)
English descriptors
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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Format Inist (serveur)
NO : | PASCAL 06-0391956 INIST |
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ET : | Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10 |
AU : | DAN SU; ZHIYONG LOU; FEI SUN; YUJIA ZHAI; HAITAO YANG; RONGGUANG ZHANG; JOACHIMIAK (Andrzej); ZHANG (Xuejun C.); BARTLAM (Mark); ZIHE RAO |
AF : | Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University/Beijing 100084/Chine (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 9 aut., 10 aut.); National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences/Beijing 100101/Chine (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 6 aut., 8 aut., 9 aut., 10 aut.); Biosciences Division, Argonne National Laboratory/Argonne, Illinois 60439/Etats-Unis (6 aut., 7 aut.); Crystallography Research Program, Oklahoma Medical Research Foundation/Oklahoma City, Oklahoma 73104/Etats-Unis (8 aut.) |
DT : | Publication en série; Niveau analytique |
SO : | Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2006; Vol. 80; No. 16; Pp. 7902-7908; Bibl. 26 ref. |
LA : | Anglais |
EA : | 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. |
CC : | 002A05C10 |
FD : | Coronavirus; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère |
FG : | Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie |
ED : | Coronavirus; Protein; Microbiology; Virology; Severe acute respiratory syndrome |
EG : | Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease |
SD : | Coronavirus; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo |
LO : | INIST-13592.354000133387600120 |
ID : | 06-0391956 |
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Pascal:06-0391956Le 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>
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<author><name sortKey="Rongguang Zhang" sort="Rongguang Zhang" uniqKey="Rongguang Zhang" last="Rongguang Zhang">RONGGUANG ZHANG</name>
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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="Zhang, Xuejun C" sort="Zhang, Xuejun C" uniqKey="Zhang X" first="Xuejun C." last="Zhang">Xuejun C. Zhang</name>
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<author><name sortKey="Bartlam, Mark" sort="Bartlam, Mark" uniqKey="Bartlam M" first="Mark" last="Bartlam">Mark Bartlam</name>
<affiliation><inist:fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
<s2>Beijing 100084</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
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<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
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</affiliation>
<affiliation><inist:fA14 i1="02"><s1>National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences</s1>
<s2>Beijing 100101</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
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</affiliation>
</author>
<author><name sortKey="Zihe Rao" sort="Zihe Rao" uniqKey="Zihe Rao" last="Zihe Rao">ZIHE RAO</name>
<affiliation><inist:fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
<s2>Beijing 100084</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
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</affiliation>
<affiliation><inist:fA14 i1="02"><s1>National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences</s1>
<s2>Beijing 100101</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
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</analytic>
<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>
</imprint>
</series>
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<seriesStmt><title level="j" type="main">Journal of virology</title>
<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
</seriesStmt>
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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>
<term>Protéine</term>
<term>Microbiologie</term>
<term>Virologie</term>
<term>Syndrome respiratoire aigu sévère</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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<fA06><s2>16</s2>
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<fA08 i1="01" i2="1" l="ENG"><s1>Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10</s1>
</fA08>
<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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<fA11 i1="03" i2="1"><s1>FEI SUN</s1>
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<fA11 i1="06" i2="1"><s1>RONGGUANG ZHANG</s1>
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<fA11 i1="08" i2="1"><s1>ZHANG (Xuejun C.)</s1>
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<fA11 i1="10" i2="1"><s1>ZIHE RAO</s1>
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<fA14 i1="01"><s1>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University</s1>
<s2>Beijing 100084</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
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<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>9 aut.</sZ>
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</fA14>
<fA14 i1="02"><s1>National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences</s1>
<s2>Beijing 100101</s2>
<s3>CHN</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
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<sZ>6 aut.</sZ>
<sZ>8 aut.</sZ>
<sZ>9 aut.</sZ>
<sZ>10 aut.</sZ>
</fA14>
<fA14 i1="03"><s1>Biosciences Division, Argonne National Laboratory</s1>
<s2>Argonne, Illinois 60439</s2>
<s3>USA</s3>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
</fA14>
<fA14 i1="04"><s1>Crystallography Research Program, Oklahoma Medical Research Foundation</s1>
<s2>Oklahoma City, Oklahoma 73104</s2>
<s3>USA</s3>
<sZ>8 aut.</sZ>
</fA14>
<fA20><s1>7902-7908</s1>
</fA20>
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<s2>13592</s2>
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<s1>© 2006 INIST-CNRS. All rights reserved.</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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<server><NO>PASCAL 06-0391956 INIST</NO>
<ET>Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10</ET>
<AU>DAN SU; ZHIYONG LOU; FEI SUN; YUJIA ZHAI; HAITAO YANG; RONGGUANG ZHANG; JOACHIMIAK (Andrzej); ZHANG (Xuejun C.); BARTLAM (Mark); ZIHE RAO</AU>
<AF>Tsinghua-IBP Joint Research Group for Structural Biology," Tsinghua University/Beijing 100084/Chine (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 9 aut., 10 aut.); National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences/Beijing 100101/Chine (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 6 aut., 8 aut., 9 aut., 10 aut.); Biosciences Division, Argonne National Laboratory/Argonne, Illinois 60439/Etats-Unis (6 aut., 7 aut.); Crystallography Research Program, Oklahoma Medical Research Foundation/Oklahoma City, Oklahoma 73104/Etats-Unis (8 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. 7902-7908; Bibl. 26 ref.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère</FD>
<FG>Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie</FG>
<ED>Coronavirus; Protein; Microbiology; Virology; Severe acute respiratory syndrome</ED>
<EG>Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease</EG>
<SD>Coronavirus; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo</SD>
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