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The crystal structure of SARS nsp10 without zinc ion as additiveThe crystal structure of SARS nsp10 without zinc ion as additive
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10.,Su D, Lou Z, Sun F, Zhai Y, Yang H, Zhang R, Joachimiak A, Zhang XC, Bartlam M, Rao Z J Virol. 2006 Aug;80(16):7902-8. PMID:16873247[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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