4l2h: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 4l2h is ON HOLD
+==Structure of a catalytically inactive PARG in complex with a poly-ADP-ribose fragment==
+<StructureSection load='4l2h' size='340' side='right'caption='[[4l2h]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4l2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L2H 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]] 1.46&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=4l2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2h OCA], [https://pdbe.org/4l2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l2h RCSB], [https://www.ebi.ac.uk/pdbsum/4l2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2h ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/I6L8L7_TETTH I6L8L7_TETTH]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Poly-ADP-ribosylation is a post-translational modification that regulates processes involved in genome stability. Breakdown of the poly(ADP-ribose) (PAR) polymer is catalysed by poly(ADP-ribose) glycohydrolase (PARG), whose endo-glycohydrolase activity generates PAR fragments. Here we present the crystal structure of PARG incorporating the PAR substrate. The two terminal ADP-ribose units of the polymeric substrate are bound in exo-mode. Biochemical and modelling studies reveal that PARG acts predominantly as an exo-glycohydrolase. This preference is linked to Phe902 (human numbering), which is responsible for low-affinity binding of the substrate in endo-mode. Our data reveal the mechanism of poly-ADP-ribosylation reversal, with ADP-ribose as the dominant product, and suggest that the release of apoptotic PAR fragments occurs at unusual PAR/PARG ratios.
-Authors: Brassington, A., Dunstan, M.S., Leys, D.
+Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities.,Barkauskaite E, Brassington A, Tan ES, Warwicker J, Dunstan MS, Banos B, Lafite P, Ahel M, Mitchison TJ, Ahel I, Leys D Nat Commun. 2013 Aug 6;4:2164. doi: 10.1038/ncomms3164. PMID:23917065<ref>PMID:23917065</ref>
-Description: Structure of a catalytically inactive PARG in complex with a poly-ADP-ribose fragment
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4l2h" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Poly(ADP-ribose) glycohydrolase 3D structures|Poly(ADP-ribose) glycohydrolase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Tetrahymena thermophila]]
+[[Category: Brassington A]]
+[[Category: Dunstan MS]]
+[[Category: Leys D]]