5zdf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:27, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5zdf' size='340' side='right'caption='[[5zdf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5zdf' size='340' side='right'caption='[[5zdf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<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>
+
<table><tr><td colspan='2'>[[5zdf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans_R1 Deinococcus radiodurans R1]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.504&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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'>[https://proteopedia.org/fgij/fg.htm?mol=5zdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zdf OCA], [https://pdbe.org/5zdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zdf RCSB], [https://www.ebi.ac.uk/pdbsum/5zdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zdf ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q9RZM4_DEIRA Q9RZM4_DEIRA]
-
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5zdf" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Poly(ADP-ribose) glycohydrolase 3D structures|Poly(ADP-ribose) glycohydrolase 3D structures]]
*[[Poly(ADP-ribose) glycohydrolase 3D structures|Poly(ADP-ribose) glycohydrolase 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Deira]]
+
[[Category: Deinococcus radiodurans R1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Cho, C C]]
+
[[Category: Cho CC]]
-
[[Category: Hsu, C H]]
+
[[Category: Hsu CH]]
-
[[Category: Adp-ribose]]
+
-
[[Category: Hydrolase]]
+

Current revision

Crystal structure of poly(ADP-ribose) glycohydrolase (PARG) T267K mutant from Deinococcus radiodurans in complex with ADP-ribose

PDB ID 5zdf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools