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4uck
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4uck is ON HOLD Authors: Paesen, G.C., Collet, A., Sallamand, C., Debart, F., Vasseur, J.J., Canard, B., Decroly, E., Grimes, J.M. Description: X-r...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray structure and activities of an essential Mononegavirales L- protein domain== | |
| + | <StructureSection load='4uck' size='340' side='right'caption='[[4uck]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4uck]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_metapneumovirus Human metapneumovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UCK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uck FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uck OCA], [https://pdbe.org/4uck PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uck RCSB], [https://www.ebi.ac.uk/pdbsum/4uck PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uck ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q91L20_9MONO Q91L20_9MONO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4uck" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human metapneumovirus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Canard B]] | ||
| + | [[Category: Collet A]] | ||
| + | [[Category: Debart F]] | ||
| + | [[Category: Decroly E]] | ||
| + | [[Category: Grimes JM]] | ||
| + | [[Category: Paesen GC]] | ||
| + | [[Category: Sallamand C]] | ||
| + | [[Category: Vasseur JJ]] | ||
Current revision
X-ray structure and activities of an essential Mononegavirales L- protein domain
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