2fqm
From Proteopedia
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Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
Overview
In the replication cycle of nonsegmented negative-strand RNA viruses, the, viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein, (N)-enwrapped RNA template during the RNA polymerase reaction. The viral, phosphoprotein (P) is a polymerase cofactor essential for this, recognition. We report here the 2.3-angstroms-resolution crystal structure, of the central domain (residues 107 to 177) of P from vesicular stomatitis, virus. The fold of this domain consists of a beta hairpin, an alpha helix, and another beta hairpin. The alpha helix provides the stabilizing force, for forming a homodimer, while the two beta hairpins add additional, stabilization by forming a four-stranded beta sheet through domain, swapping between two molecules. This central dimer positions the N- and, C-terminal domains of P to interact with the N and L proteins, allowing, the L protein to specifically recognize the nucleocapsid-RNA template and, to progress along the template while concomitantly assembling N with, nascent RNA. The interdimer interactions observed in the, noncrystallographic packing may offer insight into the mechanism of the, RNA polymerase processive reaction along the viral nucleocapsid-RNA, template.
About this Structure
2FQM is a Single protein structure of sequence from Vesicular stomatitis indiana virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus., Ding H, Green TJ, Lu S, Luo M, J Virol. 2006 Mar;80(6):2808-14. PMID:16501089
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