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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).

Original publication

DOI

10.1016/j.str.2004.01.016

Type

Journal article

Journal

Structure

Publication Date

02/2004

Volume

12

Pages

341 - 353

Keywords

Amino Acid Motifs, Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Hydrogen Bonding, Models, Molecular, Molecular Sequence Data, Protein Binding, RNA, Viral, RNA-Binding Proteins, SARS Virus, Sequence Homology, Amino Acid, Ultracentrifugation, Viral Proteins