6r0t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='6r0t' size='340' side='right'caption='[[6r0t]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='6r0t' size='340' side='right'caption='[[6r0t]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6r0t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R0T FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6r0t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Getv Getv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R0T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6R0T FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0t OCA], [http://pdbe.org/6r0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r0t RCSB], [http://www.ebi.ac.uk/pdbsum/6r0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0t ProSAT]</span></td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nsP1234 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=59300 GETV])</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6r0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0t OCA], [http://pdbe.org/6r0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r0t RCSB], [http://www.ebi.ac.uk/pdbsum/6r0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0t ProSAT]</span></td></tr>
</table>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6r0t" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Getv]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Coutard, B]]
[[Category: Coutard, B]]

Revision as of 06:11, 14 October 2020

Getah virus macro domain in complex with ADPr in open conformation

PDB ID 6r0t

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools