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1UW7

Nsp9 protein from SARS-coronavirus.

Summary for 1UW7
Entry DOI10.2210/pdb1uw7/pdb
Related1P9T 1PUK 1UJ1 1UK2 1UK3 1UK4
DescriptorNSP9 (1 entity in total)
Functional Keywordsvirus, viral protein, replicase protein, sars, coronavirus, rna-binding
Biological sourceSARS CORONAVIRUS HKU-39849
Total number of polymer chains1
Total formula weight16000.19
Authors
Primary citationSutton, G.,Fry, E.,Carter, L.,Sainsbury, S.,Walter, T.,Nettleship, J.,Berrow, N.,Owens, R.,Gilbert, R.,Davidson, A.,Siddell, S.,Poon, L.L.M.,Diprose, J.,Alderton, D.,Walsh, M.,Grimes, J.M.,Stuart, D.I.
The Nsp9 Replicase Protein of Sars-Coronavirus, Structure and Functional Insights
Structure, 12:341-, 2004
Cited by
PubMed 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).
PubMed: 14962394
DOI: 10.1016/J.STR.2004.01.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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