1vyi
From Proteopedia
|
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 ... [(full description)]
About this Structure
1VYI is a [Single protein] structure of sequence from [Rabies virus] with GOL as [ligand]. Active as [Transferase], with EC number [2.7.7.48]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 08:22:34 2007
