2pus

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[[Image:2pus.jpg|left|200px]]
 
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==Unprecedented activation mechanism of a non-canonical RNA-dependent RNA polymerase==
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The line below this paragraph, containing "STRUCTURE_2pus", creates the "Structure Box" on the page.
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<StructureSection load='2pus' size='340' side='right'caption='[[2pus]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2pus]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Infectious_bursal_disease_virus Infectious bursal disease virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PUS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PUS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pus OCA], [https://pdbe.org/2pus PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pus RCSB], [https://www.ebi.ac.uk/pdbsum/2pus PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pus ProSAT]</span></td></tr>
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{{STRUCTURE_2pus| PDB=2pus | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RDRP_IBDV RDRP_IBDV] RNA-dependent RNA polymerase which is found both free and covalently attached to the genomic RNA. May also contain guanylyl and methyl transferase activities (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pu/2pus_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pus ConSurf].
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<div style="clear:both"></div>
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'''Unprecedented activation mechanism of a non-canonical RNA-dependent RNA polymerase'''
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==See Also==
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*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Two lineages of viral RNA-dependent RNA polymerases (RDRPs) differing in the organization (canonical vs. noncanonical) of the palm subdomain have been identified. Phylogenetic analyses indicate that both lineages diverged at a very early stage of the evolution of the enzyme [Gorbalenya AE, Pringle FM, Zeddam JL, Luke BT, Cameron CE, Kalmakoff J, Hanzlik TN, Gordon KH, Ward VK (2002) J Mol Biol 324:47-62]. Here, we report the x-ray structure of a noncanonical birnaviral RDRP, named VP1, in its free form, bound to Mg(2+) ions, and bound to a peptide representing the polymerase-binding motif of the regulatory viral protein VP3. The structure of VP1 reveals that the noncanonical connectivity of the palm subdomain maintains the geometry of the catalytic residues found in canonical polymerases but results in a partial blocking of the active site cavity. The VP1-VP3 peptide complex shows a mode of polymerase activation in which VP3 binding promotes a conformational change that removes the steric blockade of the VP1 active site, facilitating the accommodation of the template and incoming nucleotides for catalysis. The striking structural similarities between birnavirus (dsRNA) and the positive-stranded RNA picornavirus and calicivirus RDRPs provide evidence supporting the existence of functional and evolutionary relationships between these two virus groups.
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[[Category: Infectious bursal disease virus]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Abaitua F]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PUS OCA].
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[[Category: Garriga D]]
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[[Category: Navarro A]]
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==Reference==
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[[Category: Querol-Audi J]]
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Activation mechanism of a noncanonical RNA-dependent RNA polymerase., Garriga D, Navarro A, Querol-Audi J, Abaitua F, Rodriguez JF, Verdaguer N, Proc Natl Acad Sci U S A. 2007 Dec 18;104(51):20540-5. Epub 2007 Dec 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18077388 18077388]
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[[Category: Rodriguez JF]]
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[[Category: Abaitua, F.]]
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[[Category: Verdaguer N]]
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[[Category: Garriga, D.]]
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[[Category: Navarro, A.]]
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[[Category: Querol-Audi, J.]]
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[[Category: Rodriguez, J F.]]
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[[Category: Verdaguer, N.]]
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[[Category: Rna polymerase motif]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:50:08 2008''
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Current revision

Unprecedented activation mechanism of a non-canonical RNA-dependent RNA polymerase

PDB ID 2pus

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