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Journal of Virology, April 2007, p. 3151-3161, Vol. 81, No. 7
0022-538X/07/$08.00+0     doi:10.1128/JVI.01939-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Novel ß-Barrel Fold in the Nuclear Magnetic Resonance Structure of the Replicase Nonstructural Protein 1 from the Severe Acute Respiratory Syndrome Coronavirus

Department of Molecular Biology, Skaggs Institute for Chemical Biology, Consortium for Functional and Structural Proteomics of the SARS-CoV, and Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037,¹ Institut für Molekularbiologie und Biophysik, ETH Zürich, CH-8093 Zürich, Switzerland²

Received 5 September 2006/ Accepted 19 December 2006

The nonstructural protein 1 (nsp1) of the severe acute respiratory syndrome coronavirus has 179 residues and is the N-terminal cleavage product of the viral replicase polyprotein that mediates RNA replication and processing. The specific function of nsp1 is not known. Here we report the nuclear magnetic resonance structure of the nsp1 segment from residue 13 to 128, which represents a novel /ß-fold formed by a mixed parallel/antiparallel six-stranded ß-barrel, an -helix covering one opening of the barrel, and a 3₁₀-helix alongside the barrel. We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered. The structure is analyzed in a search for possible correlations with the recently reported activity of nsp1 in the degradation of mRNA.

Published ahead of print on 3 January 2007.

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