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NMR Structure of the nonstructural Protein 7 (nsP7) from the SARS CoronaVirus

Overview

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 (alpha2 to alpha4) 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, 3(10)-helix, is packed across the surface of alpha2 and alpha3 in the, helix sheet, with the alpha-helical region oriented at a 60 degrees angle, relative to alpha2 and alpha3. 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 alpha1. Each of these three areas is thus, implicated as a potential site for protein-protein interactions.

About this Structure

1YSY is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.

Reference

Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7., Peti W, Johnson MA, Herrmann T, Neuman BW, Buchmeier MJ, Nelson M, Joseph J, Page R, Stevens RC, Kuhn P, Wuthrich K, J Virol. 2005 Oct;79(20):12905-13. PMID:16188992

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