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4ud0

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'''Unreleased structure'''
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==X-ray structure and activities of an essential Mononegavirales L- protein domain==
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<StructureSection load='4ud0' size='340' side='right' caption='[[4ud0]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ud0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UD0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4uci|4uci]], [[4ucj|4ucj]], [[4uck|4uck]], [[4ucl|4ucl]], [[4ucy|4ucy]], [[4ucz|4ucz]]</td></tr>
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<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=4ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud0 OCA], [http://pdbe.org/4ud0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ud0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ud0 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The L protein of mononegaviruses harbours all catalytic activities for genome replication and transcription. It contains six conserved domains (CR-I to -VI; Fig. 1a). CR-III has been linked to polymerase and polyadenylation activity, CR-V to mRNA capping and CR-VI to cap methylation. However, how these activities are choreographed is poorly understood. Here we present the 2.2-A X-ray structure and activities of CR-VI+, a portion of human Metapneumovirus L consisting of CR-VI and the poorly conserved region at its C terminus, the +domain. The CR-VI domain has a methyltransferase fold, which besides the typical S-adenosylmethionine-binding site ((SAM)P) also contains a novel pocket ((NS)P) that can accommodate a nucleoside. CR-VI lacks an obvious cap-binding site, and the (SAM)P-adjoining site holding the nucleotides undergoing methylation ((SUB)P) is unusually narrow because of the overhanging +domain. CR-VI+ sequentially methylates caps at their 2'O and N7 positions, and also displays nucleotide triphosphatase activity.
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The entry 4ud0 is ON HOLD until Paper Publication
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X-ray structure and activities of an essential Mononegavirales L-protein domain.,Paesen GC, Collet A, Sallamand C, Debart F, Vasseur JJ, Canard B, Decroly E, Grimes JM Nat Commun. 2015 Nov 9;6:8749. doi: 10.1038/ncomms9749. PMID:26549102<ref>PMID:26549102</ref>
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Authors: Paesen, G.C., Collet, A., Sallamand, C., Debart, F., Vasseur, J.J., Canard, B., Decroly, E., Grimes, J.M.
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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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Description: X-ray structure and activities of an essential Mononegavirales L-protein domain
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<div class="pdbe-citations 4ud0" style="background-color:#fffaf0;"></div>
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[[Category: Unreleased Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Canard, B]]
[[Category: Canard, B]]
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[[Category: Sallamand, C]]
 
[[Category: Collet, A]]
[[Category: Collet, A]]
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[[Category: Paesen, G.C]]
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[[Category: Debart, F]]
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[[Category: Grimes, J.M]]
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[[Category: Vasseur, J.J]]
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[[Category: Decroly, E]]
[[Category: Decroly, E]]
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[[Category: Debart, F]]
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[[Category: Grimes, J M]]
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[[Category: Paesen, G C]]
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[[Category: Sallamand, C]]
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[[Category: Vasseur, J J]]
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[[Category: Capping]]
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[[Category: L protein]]
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[[Category: Rossmann]]
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[[Category: Transferase]]
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[[Category: Triphosphatase]]

Revision as of 18:55, 1 December 2015

X-ray structure and activities of an essential Mononegavirales L- protein domain

4ud0, resolution 3.20Å

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