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==X-ray structure and activities of an essential Mononegavirales L- protein domain==
<StructureSection load='4ucl' size='340' side='right'caption='[[4ucl]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ucl]] 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=4UCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UCL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4ucl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ucl OCA], [https://pdbe.org/4ucl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ucl RCSB], [https://www.ebi.ac.uk/pdbsum/4ucl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ucl 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ucl" 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]]