JVI Accepts, published online ahead of print on 29 August 2007
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J. Virol. doi:10.1128/JVI.00969-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

NMR Structure of the N-terminal Domain of the Nonstructural Protein 3 from the SARS Coronavirus

Pedro Serrano, Margaret A. Johnson, Marcius S. Almeida, Reto Horst, Torsten Herrmann, Jeremiah S. Joseph, Benjamin W. Neuman, Vanitha Subramanian, Kumar S. Saikatendu, Michael J. Buchmeier, Raymond C. Stevens, Peter Kuhn, and Kurt Wüthrich*

Departments of Molecular Biology, Molecular and Integrative Neurosciences, Cell Biology, and Chemistry, Skaggs Institute for Chemical Biology, and Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA; Institute for Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland

* To whom correspondence should be addressed. Email: wuthrich{at}scripps.edu.


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Abstract

This paper describes the structure determination of nsp3a, the N-terminal domain of the SARS-CoV non-structural protein 3. Nsp3a exhibits an ubiquitin-like globular fold of residues 1–112, and a flexibly extended glutamic acid-rich domain of residues 113–183. In addition to the four {beta}-strands and two {alpha}-helices that are common to ubiquitin-like folds, the globular domain of nsp3a contains two short helices representing a feature that has not previously been observed in these proteins. NMR chemical shift perturbations showed that these unique structural elements are involved in interactions with single-stranded RNA. Structural similarities with proteins involved in various cell-signaling pathways indicate possible roles of nsp3a in viral infection and persistence.




This article has been cited by other articles:

  • Serrano, P., Johnson, M. A., Chatterjee, A., Neuman, B. W., Joseph, J. S., Buchmeier, M. J., Kuhn, P., Wuthrich, K. (2009). Nuclear Magnetic Resonance Structure of the Nucleic Acid-Binding Domain of Severe Acute Respiratory Syndrome Coronavirus Nonstructural Protein 3. J. Virol. 83: 12998-13008 [Abstract] [Full Text]  
  • Chatterjee, A., Johnson, M. A., Serrano, P., Pedrini, B., Joseph, J. S., Neuman, B. W., Saikatendu, K., Buchmeier, M. J., Kuhn, P., Wuthrich, K. (2009). Nuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain Fold. J. Virol. 83: 1823-1836 [Abstract] [Full Text]  
  • Neuman, B. W., Joseph, J. S., Saikatendu, K. S., Serrano, P., Chatterjee, A., Johnson, M. A., Liao, L., Klaus, J. P., Yates, J. R. III, Wuthrich, K., Stevens, R. C., Buchmeier, M. J., Kuhn, P. (2008). Proteomics Analysis Unravels the Functional Repertoire of Coronavirus Nonstructural Protein 3. J. Virol. 82: 5279-5294 [Abstract] [Full Text]  


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