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.
Su
Dan
D
Tsinghua-IBP Joint Research Group for Structural Biology, Tsinghua University, Beijing 100084, China.
Lou
Zhiyong
Z
Sun
Fei
F
Zhai
Yujia
Y
Yang
Haitao
H
Zhang
Rongguang
R
Joachimiak
Andrzej
A
Zhang
Xuejun C
XC
Bartlam
Mark
M
Rao
Zihe
Z
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D045473:Severe acute respiratory syndrome-related coronavirus / Q000235:genetics / Q000502:physiology*; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D016335:Zinc Fingers
D014157:Transcription Factors; D017361:Viral Nonstructural Proteins