2wzl

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(New page: '''Unreleased structure''' The entry 2wzl is ON HOLD Authors: Assenberg, R., Delmas, O., Ren, J., Vidalain, P., Verma, A., Larrous, F., Graham, S., Tangy, F., Grimes, J., Bourhy, H. De...)
Current revision (10:20, 20 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2wzl is ON HOLD
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==The Structure of the N-RNA Binding Domain of the Mokola virus Phosphoprotein==
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<StructureSection load='2wzl' size='340' side='right'caption='[[2wzl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2wzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mokola_lyssavirus Mokola lyssavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WZL FirstGlance]. <br>
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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]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2wzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wzl OCA], [https://pdbe.org/2wzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wzl RCSB], [https://www.ebi.ac.uk/pdbsum/2wzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wzl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHOSP_MOKV PHOSP_MOKV] Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (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/wz/2wzl_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=2wzl ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mokola virus (MOKV) is a nonsegmented, negative-sense RNA virus that belongs to the Lyssavirus genus and Rhabdoviridae family. MOKV phosphoprotein P is an essential component of the replication and transcription complex and acts as a cofactor for the viral RNA-dependent RNA polymerase. P recruits the viral polymerase to the nucleoprotein-bound viral RNA (N-RNA) via an interaction between its C-terminal domain and the N-RNA complex. Here we present a structure for this domain of MOKV P, obtained by expression of full-length P in Escherichia coli, which was subsequently truncated during crystallization. The structure has a high degree of homology with P of rabies virus, another member of Lyssavirus genus, and to a lesser degree with P of vesicular stomatitis virus (VSV), a member of the related Vesiculovirus genus. In addition, analysis of the crystal packing of this domain reveals a potential binding site for the nucleoprotein N. Using both site-directed mutagenesis and yeast two-hybrid experiments to measure P-N interaction, we have determined the relative roles of key amino acids involved in this interaction to map the region of P that binds N. This analysis also reveals a structural relationship between the N-RNA binding domain of the P proteins of the Rhabdoviridae and the Paramyxoviridae.
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Authors: Assenberg, R., Delmas, O., Ren, J., Vidalain, P., Verma, A., Larrous, F., Graham, S., Tangy, F., Grimes, J., Bourhy, H.
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Structure of the nucleoprotein binding domain of Mokola virus phosphoprotein.,Assenberg R, Delmas O, Ren J, Vidalain PO, Verma A, Larrous F, Graham SC, Tangy F, Grimes JM, Bourhy H J Virol. 2010 Jan;84(2):1089-96. Epub 2009 Nov 11. PMID:19906936<ref>PMID:19906936</ref>
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Description: The Structure of the N-RNA Binding Domain of the Mokola virus Phosphoprotein
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 9 14:39:13 2009''
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<div class="pdbe-citations 2wzl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mokola lyssavirus]]
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[[Category: Assenberg R]]
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[[Category: Bourhy H]]
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[[Category: Delmas O]]
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[[Category: Graham S]]
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[[Category: Grimes J]]
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[[Category: Larrous F]]
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[[Category: Ren J]]
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[[Category: Tangy F]]
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[[Category: Verma A]]
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[[Category: Vidalain P]]

Current revision

The Structure of the N-RNA Binding Domain of the Mokola virus Phosphoprotein

PDB ID 2wzl

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