4ud0: Difference between revisions
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==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ud0]] is a 1 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=4UD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UD0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ud0 OCA], [https://pdbe.org/4ud0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ud0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ud0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ud0 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> | |||
[[Category: | </div> | ||
[[Category: Canard | <div class="pdbe-citations 4ud0" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
[[Category: Grimes | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </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]] | |||
Latest revision as of 14:19, 9 May 2024
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
FunctionPublication 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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