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Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3

Serrano, P., Johnson, M. A., Chatterjee, A., Neuman, B. W., Joseph, J. S., Buchmeier, M. J., Kuhn, P. and Wuthrich, K. (2009) Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3. Journal of Virology, 83 (24). pp. 12998-13008. ISSN 0022-538X

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To link to this article DOI: 10.1128/jvi.01253-09

Abstract/Summary

The nuclear magnetic resonance (NMR) structure of a globular domain of residues 1071 to 1178 within the previously annotated nucleic acid-binding region (NAB) of severe acute respiratory syndrome coronavirus nonstructural protein 3 (nsp3) has been determined, and N- and C-terminally adjoining polypeptide segments of 37 and 25 residues, respectively, have been shown to form flexibly extended linkers to the preceding globular domain and to the following, as yet uncharacterized domain. This extension of the structural coverage of nsp3 was obtained from NMR studies with an nsp3 construct comprising residues 1066 to 1181 [ nsp3(1066-1181)] and the constructs nsp3(1066-1203) and nsp3(1035-1181). A search of the protein structure database indicates that the globular domain of the NAB represents a new fold, with a parallel four-strand beta-sheet holding two alpha-helices of three and four turns that are oriented antiparallel to the beta-strands. Two antiparallel two-strand beta-sheets and two 3(10)-helices are anchored against the surface of this barrel-like molecular core. Chemical shift changes upon the addition of single-stranded RNAs (ssRNAs) identified a group of residues that form a positively charged patch on the protein surface as the binding site responsible for the previously reported affinity for nucleic acids. This binding site is similar to the ssRNA-binding site of the sterile alpha motif domain of the Saccharomyces cerevisiae Vts1p protein, although the two proteins do not share a common globular fold.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Biological Sciences > Biomedical Sciences
ID Code:9694
Uncontrolled Keywords:Amino Acid Sequence Binding Sites Magnetic Resonance Spectroscopy Molecular Conformation Molecular Sequence Data Protein Structure, Secondary Protein Structure, Tertiary RNA/*metabolism RNA Replicase/*chemistry Viral Nonstructural Proteins/*chemistry
Additional Information:Serrano, Pedro Johnson, Margaret A Chatterjee, Amarnath Neuman, Benjamin W Joseph, Jeremiah S Buchmeier, Michael J Kuhn, Peter Wuthrich, Kurt AI059799/AI/NIAID NIH HHS/United States U54-GM074898/GM/NIGMS NIH HHS/United States Canadian Institutes of Health Research/Canada Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't United States Journal of virology J Virol. 2009 Dec;83(24):12998-3008. Epub 2009 Oct 14.
Publisher:American Society for Microbiology

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