4ud0: Difference between revisions
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==X-ray structure and activities of an essential Mononegavirales L- protein domain== | ==X-ray structure and activities of an essential Mononegavirales L- protein domain== | ||
<StructureSection load='4ud0' size='340' side='right' caption='[[4ud0]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='4ud0' size='340' side='right'caption='[[4ud0]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <table><tr><td colspan='2'>[[4ud0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hmpv Hmpv]. 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> | ||
</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> | </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> | ||
<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> | <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> | ||
<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> | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ud0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4ud0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ud0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[RNA polymerase|RNA polymerase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Hmpv]] | |||
[[Category: Large Structures]] | |||
[[Category: Canard, B]] | [[Category: Canard, B]] | ||
[[Category: Collet, A]] | [[Category: Collet, A]] | ||
Revision as of 10:29, 24 April 2019
X-ray structure and activities of an essential Mononegavirales L- protein domainX-ray structure and activities of an essential Mononegavirales L- protein domain
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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