1vyi
From Proteopedia
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STRUCTURE OF THE C-TERMINAL DOMAIN OF THE POLYMERASE COFACTOR OF RABIES VIRUS: INSIGHTS IN FUNCTION AND EVOLUTION.
Overview
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.
About this Structure
1VYI is a Single protein structure of sequence from Rabies virus with as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus., Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW, J Mol Biol. 2004 Oct 29;343(4):819-31. PMID:15476803
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