6r0r: Difference between revisions
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The | ==Getah virus macro domain in complex with ADPr covalently bond to Cys34== | ||
<StructureSection load='6r0r' size='340' side='right'caption='[[6r0r]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6r0r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Getah_virus Getah virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R0R 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]] 1.45Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=JNT:[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]+[(2~{R},3~{S},4~{S})-2,3,4,5-tetrakis(oxidanyl)pentyl]+hydrogen+phosphate'>JNT</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=6r0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0r OCA], [https://pdbe.org/6r0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r0r RCSB], [https://www.ebi.ac.uk/pdbsum/6r0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0r ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Alphaviruses are (re-)emerging arboviruses of public health concern. The nsP3 gene product is one of the key players during viral replication. NsP3 comprises three domains: a macro domain, a zinc-binding domain and a hypervariable region. The macro domain is essential at both early and late stages of the replication cycle through ADP-ribose (ADPr) binding and de-ADP-ribosylation of host proteins. However, both its specific role and the precise molecular mechanism of de-ADP-ribosylation across specific viral families remains to be elucidated. Here we investigate by X-ray crystallography the mechanism of ADPr reactivity in the active site of Getah virus macro domain, which displays a peculiar substitution of one of the conserved residues in the catalytic loop. ADPr adopts distinct poses including a covalent bond between the C''1 of the ADPr and a conserved Togaviridae-specific cysteine. These different poses observed for ADPr may represent snapshots of the de-ADP-ribosylation mechanism, highlighting residues to be further characterised. | |||
Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography.,Ferreira-Ramos AS, Sulzenbacher G, Canard B, Coutard B Sci Rep. 2020 Sep 2;10(1):14422. doi: 10.1038/s41598-020-70870-w. PMID:32879358<ref>PMID:32879358</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6r0r" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Sulzenbacher | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Getah virus]] | |||
[[Category: Large Structures]] | |||
[[Category: Coutard B]] | |||
[[Category: Ferreira Ramos AS]] | |||
[[Category: Sulzenbacher G]] | |||
