3HHZ

Complex of the vesicular stomatitis virus nucleocapsid and the nucleocapsid-binding domain of the phosphoprotein

Summary for 3HHZ

• Entry DOI: 10.2210/pdb3hhz/pdb
• Related: 3HHW
• Descriptor: Phosphoprotein, Nucleoprotein, RNA (45-MER) (3 entities in total)
• Functional Keywords: protein, rna, template, replication, negative strand rna virus, chaperone, phosphoprotein, rna replication, virion, ribonucleoprotein, rna-binding, viral nucleoprotein, viral protein, viral protein-rna complex, viral protein/rna
• Biological source: Vesicular stomatitis Indiana virus (VSIV); More
• Cellular location: Virion: P04880 Q77E03
• Total number of polymer chains: 11
• Total formula weight: 299362.50

Authors

Green, T.J.,Luo, M. (deposition date: 2009-05-18, release date: 2009-07-28, Last modification date: 2023-09-06)

Primary citation

Green, T.J.,Luo, M.
Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P.
Proc.Natl.Acad.Sci.USA, 106:11713-11718, 2009

PubMed Abstract: The negative-strand RNA viruses (NSRVs) are unique because their nucleocapsid, not the naked RNA, is the active template for transcription and replication. The viral polymerase of nonsegmented NSRVs contains a large polymerase catalytic subunit (L) and a nonenzymatic cofactor, the phosphoprotein (P). Insight into how P delivers the polymerase complex to the nucleocapsid has long been pursued by reverse genetics and biochemical approaches. Here, we present the X-ray crystal structure of the C-terminal domain of P of vesicular stomatitis virus, a prototypic nonsegmented NSRV, bound to nucleocapsid-like particles. P binds primarily to the C-terminal lobe of 2 adjacent N proteins within the nucleocapsid. This binding mode is exclusive to the nucleocapsid, not the nucleocapsid (N) protein in other existing forms. Localization of phosphorylation sites within P and their proximity to the RNA cavity give insight into how the L protein might be oriented to access the RNA template.

PubMed: 19571006
DOI: 10.1073/pnas.0903228106

Experimental method

X-RAY DIFFRACTION (3.5 Å)