Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.
Identifieur interne : 002153 ( PubMed/Corpus ); précédent : 002152; suivant : 002154Dodecamer 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.
English descriptors
- KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, SARS Virus (genetics), SARS Virus (physiology), Transcription Factors (chemistry), Transcription Factors (genetics), Transcription Factors (physiology), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (physiology), Zinc Fingers.
- MESH :
- chemical , chemistry : Transcription Factors, Viral Nonstructural Proteins.
- genetics : SARS Virus, Transcription Factors, Viral Nonstructural Proteins.
- physiology : SARS Virus, Transcription Factors, Viral Nonstructural Proteins.
- Amino Acid Sequence, Crystallography, X-Ray, Molecular Sequence Data, Protein Conformation, Protein Folding, Zinc Fingers.
Abstract
The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 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-A 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.
DOI: 10.1128/JVI.00483-06
PubMed: 16873247
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pubmed:16873247Le document en format XML
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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 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-A 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.</div>
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<Abstract><AbstractText>The severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural proteins nsp1 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-A 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.</AbstractText>
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