2fqm

<StructureSection load='2fqm' size='340' side='right' caption='[[2fqm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[2fqm]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Vsiv Vsiv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FQM FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11277 VSIV])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqm OCA], [http://pdbe.org/2fqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fqm RCSB], [http://www.ebi.ac.uk/pdbsum/2fqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fqm ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PHOSP_VSIVM 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).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/2fqm_consurf.spt"</scriptWhenChecked>

<div style="background-color:#fffaf0;">

== 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<ref>PMID:16501089</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2fqm" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Vsiv]]

[[Category: Ding, H]]

[[Category: Green, T J]]

[[Category: Lu, S]]

[[Category: Luo, M]]

[[Category: Viral protein]]