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Journal of Virology, October 2005, p. 12905-12913, Vol. 79, No. 20
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.20.12905-12913.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Structural Genomics of the Severe Acute Respiratory Syndrome Coronavirus: Nuclear Magnetic Resonance Structure of the Protein nsP7

Wolfgang Peti,1,2,{dagger} Margaret A. Johnson,1,2 Torsten Herrmann,1,{ddagger} Benjamin W. Neuman,2,3 Michael J. Buchmeier,2,3 Mike Nelson,1,2 Jeremiah Joseph,2,4 Rebecca Page,1,5,§ Raymond C. Stevens,1,2,5 Peter Kuhn,2,4,5* and Kurt Wüthrich1,2,5*

Department of Molecular Biology,1 Consortium for Functional and Structural Proteomics of SARS-CoV Related Proteins,2 Department of Neuropharmacology,3 Department of Cell Biology,4 Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, California 920375

Received 9 June 2005/ Accepted 22 July 2005

Here, we report the three-dimensional structure of severe acute respiratory syndrome coronavirus (SARS-CoV) nsP7, a component of the SARS-CoV replicase polyprotein. The coronavirus replicase carries out regulatory tasks involved in the maintenance, transcription, and replication of the coronavirus genome. nsP7 was found to assume a compact architecture in solution, which is comprised primarily of helical secondary structures. Three helices ({alpha}2 to {alpha}4) form a flat up-down-up antiparallel {alpha}-helix sheet. The N-terminal segment of residues 1 to 22, containing two turns of {alpha}-helix and one turn of 310-helix, is packed across the surface of {alpha}2 and {alpha}3 in the helix sheet, with the {alpha}-helical region oriented at a 60° angle relative to {alpha}2 and {alpha}3. The surface charge distribution is pronouncedly asymmetrical, with the flat surface of the helical sheet showing a large negatively charged region adjacent to a large hydrophobic patch and the opposite side containing a positively charged groove that extends along the helix {alpha}1. Each of these three areas is thus implicated as a potential site for protein-protein interactions.

* Corresponding author. Mailing address for Peter Kuhn: Department of Cell Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., CB-265, La Jolla, CA 92037. Phone: (858) 784-9114. Fax: (858) 784-8996. E-mail: pkuhn{at}scripps.edu. Mailing address for Kurt Wüthrich: Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Rd., MB-44, La Jolla, CA 92037. Phone: (858) 784-8011. Fax: (858) 784-8014. E-mail: wuthrich{at}scripps.edu.

{dagger} Present address: Brown University, Department of Molecular Pharmacology, Physiology and Biotechnology, 70 Ship Street, GE-3, Providence, RI 02912.

{ddagger} Present address: Institut für Molekularbiologie und Biophysik, ETH Zürich, CH-8093 Zürich, Switzerland.

§ Present address: Brown University, Department of Molecular Biology, Cell Biology and Biochemistry, 70 Ship Street, GE-4, Providence, RI 02912.

Journal of Virology, October 2005, p. 12905-12913, Vol. 79, No. 20
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.20.12905-12913.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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