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J Mol Biol. 2004 Oct 29;343(4):819-31.

Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus.

Author information

1
EMBL Grenoble Outstation, BP181, 38042 Grenoble Cedex 9, France.

Abstract

The phosphoprotein (P) of rabies virus binds the viral polymerase to the nucleoprotein (N)-RNA template for transcription and replication. By limited protease digestion we defined a monomeric C-terminal domain of P that can bind to N-RNA. The atomic structure of this domain was determined and previously described mutations that interfere with binding of P to N-RNA could now be interpreted. There appears to be two features involved in this activity situated at opposite surfaces of the molecule: a positively charged patch and a hydrophobic pocket with an exposed tryptophan side-chain. Other previously published work suggests a conformational change in P when it binds to N-RNA, which may imply the repositioning of two helices that would expose a hydrophobic groove for interaction with N. This domain of rabies virus P is structurally unrelated to the N-RNA binding domains of the phosphoproteins of Sendai and measles virus that are members of the same order of viruses, the non-segmented negative strand RNA viruses. The implications of this finding for the evolution of this virus group are discussed.

PMID:
15476803
DOI:
10.1016/j.jmb.2004.08.071
[Indexed for MEDLINE]

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