2fqm | pdb_00002fqm

Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus

spinqualitylabelsall models 2fqm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fqm is a 6 chain structure with sequence from Vsiv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: P (VSIV) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PHOSP_VSIVM] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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