Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.

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.
AuthorsDan Su, Zhiyong Lou, Fei Sun, Yujia Zhai, Haitao Yang, Rongguang Zhang, Andrzej Joachimiak, Xuejun C Zhang, Mark Bartlam, Zihe Rao
JournalJournal of virology (J Virol) Vol. 80 Issue 16 Pg. 7902-8 (Aug 2006) ISSN: 0022-538X [Print] United States
PMID16873247 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Transcription Factors
  • Viral Nonstructural Proteins
  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • SARS Virus (genetics, physiology)
  • Transcription Factors (chemistry, genetics, physiology)
  • Viral Nonstructural Proteins (chemistry, genetics, physiology)
  • Zinc Fingers

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