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J Mol Biol. 2012 Oct 19;423(2):182-97. doi: 10.1016/j.jmb.2012.07.003. Epub 2012 Jul 9.

Ensemble structure of the modular and flexible full-length vesicular stomatitis virus phosphoprotein.

Author information

1
Unit of Virus Host Cell Interactions, UMI 3265 UJF-EMBL-CNRS, 6 rue Jules Horowitz, BP 181, 38042 Grenoble Cedex 9, France.

Abstract

The phosphoprotein (P) is an essential component of the viral replication machinery of non-segmented negative-strand RNA viruses, connecting the viral polymerase to its nucleoprotein-RNA template and acting as a chaperone of the nucleoprotein by preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of vesicular stomatitis virus (VSV) forms homodimers and possesses a modular organization comprising two stable, well-structured domains concatenated with two intrinsically disordered regions. Here, we used a combination of nuclear magnetic resonance spectroscopy and small-angle X-ray scattering to depict VSV P as an ensemble of continuously exchanging conformers that captures the dynamic character of this protein. We discuss the implications of the dynamics and the large conformational space sampled by VSV P in the assembly and functioning of the viral transcription/replication machinery.

PMID:
22789567
DOI:
10.1016/j.jmb.2012.07.003
[Indexed for MEDLINE]

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