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 Ding, H.
Right arrow Articles by Luo, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ding, H.
Right arrow Articles by Luo, M.

 Previous Article  |  Next Article 

Journal of Virology, March 2006, p. 2808-2814, Vol. 80, No. 6
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.6.2808-2814.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Crystal Structure of the Oligomerization Domain of the Phosphoprotein of Vesicular Stomatitis Virus

Haitao Ding, Todd J. Green, Shanyun Lu, and Ming Luo*

Department of Microbiology, School of Medicine, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, Alabama 35294

Received 29 September 2005/ Accepted 13 December 2005

In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-Å-resolution crystal structure of the central domain (residues 107 to 177) of P from vesicular stomatitis virus. The fold of this domain consists of a ß hairpin, an {alpha} helix, and another ß hairpin. The {alpha} helix provides the stabilizing force for forming a homodimer, while the two ß hairpins add additional stabilization by forming a four-stranded ß sheet through domain swapping between two molecules. This central dimer positions the N- and C-terminal domains of P to interact with the N and L proteins, allowing the L protein to specifically recognize the nucleocapsid-RNA template and to progress along the template while concomitantly assembling N with nascent RNA. The interdimer interactions observed in the noncrystallographic packing may offer insight into the mechanism of the RNA polymerase processive reaction along the viral nucleocapsid-RNA template.


* Corresponding author. Mailing address: Room 111, CBSE, 1025 18th Street South, University of Alabama at Birmingham, Birmingham, AL 35294. Phone: (205) 934-4259. Fax: (205) 975-9578. E-mail: mingluo{at}uab.edu.


Journal of Virology, March 2006, p. 2808-2814, Vol. 80, No. 6
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.6.2808-2814.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Zhang, X., Green, T. J., Tsao, J., Qiu, S., Luo, M. (2008). Role of Intermolecular Interactions of Vesicular Stomatitis Virus Nucleoprotein in RNA Encapsidation. J. Virol. 82: 674-682 [Abstract] [Full Text]  
  • Chen, M., Ogino, T., Banerjee, A. K. (2007). Interaction of Vesicular Stomatitis Virus P and N Proteins: Identification of Two Overlapping Domains at the N Terminus of P That Are Involved in N0-P Complex Formation and Encapsidation of Viral Genome RNA. J. Virol. 81: 13478-13485 [Abstract] [Full Text]