6r0r

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<StructureSection load='6r0r' size='340' side='right'caption='[[6r0r]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
<StructureSection load='6r0r' size='340' side='right'caption='[[6r0r]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6r0r]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R0R FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<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=6r0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r0r OCA], [http://pdbe.org/6r0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r0r RCSB], [http://www.ebi.ac.uk/pdbsum/6r0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r0r ProSAT]</span></td></tr>
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<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>
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<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>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6r0r" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
 
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[[Category: Coutard, B]]
 
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[[Category: Ramos, A S.Ferreira]]
 
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[[Category: Sulzenbacher, G]]
 
[[Category: Getah virus]]
[[Category: Getah virus]]
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[[Category: Macro domain]]
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[[Category: Large Structures]]
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[[Category: Viral protein]]
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[[Category: Coutard B]]
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[[Category: Ferreira Ramos AS]]
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[[Category: Sulzenbacher G]]

Current revision

Getah virus macro domain in complex with ADPr covalently bond to Cys34

PDB ID 6r0r

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