This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Serrano, P.
Right arrow Articles by Wüthrich, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Serrano, P.
Right arrow Articles by Wüthrich, K.

 Previous Article  |  Next Article 

Journal of Virology, November 2007, p. 12049-12060, Vol. 81, No. 21
0022-538X/07/$08.00+0     doi:10.1128/JVI.00969-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Nuclear Magnetic Resonance Structure of the N-Terminal Domain of Nonstructural Protein 3 from the Severe Acute Respiratory Syndrome Coronavirus{triangledown}

Pedro Serrano,1,5 Margaret A. Johnson,1,5,6 Marcius S. Almeida,1,5 Reto Horst,1,6 Torsten Herrmann,7 Jeremiah S. Joseph,3 Benjamin W. Neuman,2 Vanitha Subramanian,3 Kumar S. Saikatendu,3 Michael J. Buchmeier,2 Raymond C. Stevens,1 Peter Kuhn,3 and Kurt Wüthrich1,4,5,6*

Departments of Molecular Biology,1 Molecular and Integrative Neurosciences,2 Cell Biology,3 Chemistry,4 Skaggs Institute for Chemical Biology,5 Joint Center for Structural Genomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037,6 Institute for Molecular Biology and Biophysics, ETH Zürich, CH-8093 Zürich, Switzerland7

Received 4 May 2007/ Accepted 1 August 2007

This paper describes the structure determination of nsp3a, the N-terminal domain of the severe acute respiratory syndrome coronavirus (SARS-CoV) nonstructural protein 3. nsp3a exhibits a ubiquitin-like globular fold of residues 1 to 112 and a flexibly extended glutamic acid-rich domain of residues 113 to 183. In addition to the four ß-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. Nuclear magnetic resonance 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.

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

{triangledown} Published ahead of print on 29 August 2007.

Journal of Virology, November 2007, p. 12049-12060, Vol. 81, No. 21
0022-538X/07/$08.00+0     doi:10.1128/JVI.00969-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»