5zdf
From Proteopedia
(Difference between revisions)
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==Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) T267K mutant from Deinococcus radiodurans in complex with ADP-ribose== | ==Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) T267K mutant from Deinococcus radiodurans in complex with ADP-ribose== | ||
| - | <StructureSection load='5zdf' size='340' side='right' caption='[[5zdf]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='5zdf' size='340' side='right'caption='[[5zdf]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zdf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZDF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zdf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Deira Deira]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZDF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZDF FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AR6:[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL]+HYDROGEN+PHOSPHATE'>AR6</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AR6:[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL]+HYDROGEN+PHOSPHATE'>AR6</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DR_B0099 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243230 DEIRA])</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=5zdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zdf OCA], [http://pdbe.org/5zdf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zdf RCSB], [http://www.ebi.ac.uk/pdbsum/5zdf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zdf ProSAT]</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=5zdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zdf OCA], [http://pdbe.org/5zdf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zdf RCSB], [http://www.ebi.ac.uk/pdbsum/5zdf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zdf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Poly-ADP-ribosylation, a post-translational modification involved in various cellular processes, is well characterized in eukaryotes but thought to be devoid in bacteria. Here, we solve crystal structures of ADP-ribose-bound poly(ADP-ribose)glycohydrolase from the radioresistant bacterium Deinococcus radiodurans (DrPARG), revealing a solvent-accessible 2'-hydroxy group of ADP-ribose, which suggests that DrPARG may possess endo-glycohydrolase activity toward poly-ADP-ribose (PAR). We confirm the existence of PAR in D. radiodurans and show that disruption of DrPARG expression causes accumulation of endogenous PAR and compromises recovery from UV radiation damage. Moreover, endogenous PAR levels in D. radiodurans are elevated after UV irradiation, indicating that PARylation may be involved in resistance to genotoxic stresses. These findings provide structural insights into a bacterial-type PARG and suggest the existence of a prokaryotic PARylation machinery that may be involved in stress responses. | ||
| + | |||
| + | Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans.,Cho CC, Chien CY, Chiu YC, Lin MH, Hsu CH Nat Commun. 2019 Apr 2;10(1):1491. doi: 10.1038/s41467-019-09153-6. PMID:30940816<ref>PMID:30940816</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zdf" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Poly(ADP-ribose) glycohydrolase 3D structures|Poly(ADP-ribose) glycohydrolase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Deira]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Cho, C C]] | [[Category: Cho, C C]] | ||
[[Category: Hsu, C H]] | [[Category: Hsu, C H]] | ||
[[Category: Adp-ribose]] | [[Category: Adp-ribose]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 07:49, 11 March 2020
Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) T267K mutant from Deinococcus radiodurans in complex with ADP-ribose
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Categories: Deira | Large Structures | Cho, C C | Hsu, C H | Adp-ribose | Hydrolase
