| Literature DB >> 14962394 |
Geoff Sutton1, Elizabeth Fry, Lester Carter, Sarah Sainsbury, Tom Walter, Joanne Nettleship, Nick Berrow, Ray Owens, Robert Gilbert, Andrew Davidson, Stuart Siddell, Leo L M Poon, Jonathan Diprose, David Alderton, Martin Walsh, Jonathan M Grimes, David I Stuart.
Abstract
As part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV) proteins, we have solved the structure of the non-structural protein 9 (nsp9). This protein, encoded by ORF1a, has no designated function but is most likely involved with viral RNA synthesis. The protein comprises a single beta-barrel with a fold previously unseen in single domain proteins. The fold superficially resembles an OB-fold with a C-terminal extension and is related to both of the two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine protease superfamily). nsp9 has, presumably, evolved from a protease. The crystal structure suggests that the protein is dimeric. This is confirmed by analytical ultracentrifugation and dynamic light scattering. We show that nsp9 binds RNA and interacts with nsp8, activities that may be essential for its function(s).Entities:
Mesh：
Substances：
Year: 2004 PMID： 14962394 PMCID： PMC7135010 DOI： 10.1016/j.str.2004.01.016
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006