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3sih

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==The X-ray crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Thermomonospora curvata==
==The X-ray crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Thermomonospora curvata==
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<StructureSection load='3sih' size='340' side='right' caption='[[3sih]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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<StructureSection load='3sih' size='340' side='right'caption='[[3sih]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sih]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thecd Thecd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SIH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sih]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata_DSM_43183 Thermomonospora curvata DSM 43183]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIH FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sig|3sig]], [[3sii|3sii]], [[3sij|3sij]]</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]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tcur_1721 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=471852 THECD])</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=3sih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sih OCA], [https://pdbe.org/3sih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sih RCSB], [https://www.ebi.ac.uk/pdbsum/3sih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sih ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Poly(ADP-ribose)_glycohydrolase Poly(ADP-ribose) glycohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.143 3.2.1.143] </span></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=3sih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sih OCA], [http://pdbe.org/3sih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sih RCSB], [http://www.ebi.ac.uk/pdbsum/3sih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sih ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/D1AC29_THECD D1AC29_THECD]
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Post-translational modification of proteins by poly(ADP-ribosyl)ation regulates many cellular pathways that are critical for genome stability, including DNA repair, chromatin structure, mitosis and apoptosis. Poly(ADP-ribose) (PAR) is composed of repeating ADP-ribose units linked via a unique glycosidic ribose-ribose bond, and is synthesized from NAD by PAR polymerases. PAR glycohydrolase (PARG) is the only protein capable of specific hydrolysis of the ribose-ribose bonds present in PAR chains; its deficiency leads to cell death. Here we show that filamentous fungi and a number of bacteria possess a divergent form of PARG that has all the main characteristics of the human PARG enzyme. We present the first PARG crystal structure (derived from the bacterium Thermomonospora curvata), which reveals that the PARG catalytic domain is a distant member of the ubiquitous ADP-ribose-binding macrodomain family. High-resolution structures of T. curvata PARG in complexes with ADP-ribose and the PARG inhibitor ADP-HPD, complemented by biochemical studies, allow us to propose a model for PAR binding and catalysis by PARG. The insights into the PARG structure and catalytic mechanism should greatly improve our understanding of how PARG activity controls reversible protein poly(ADP-ribosyl)ation and potentially of how the defects in this regulation are linked to human disease.
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The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase.,Slade D, Dunstan MS, Barkauskaite E, Weston R, Lafite P, Dixon N, Ahel M, Leys D, Ahel I Nature. 2011 Sep 4. doi: 10.1038/nature10404. PMID:21892188<ref>PMID:21892188</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 3sih" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Poly (ADP-ribose) glycohydrolase|Poly (ADP-ribose) glycohydrolase]]
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*[[Poly(ADP-ribose) glycohydrolase 3D structures|Poly(ADP-ribose) glycohydrolase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Thecd]]
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[[Category: Large Structures]]
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[[Category: Dunstan, M S]]
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[[Category: Thermomonospora curvata DSM 43183]]
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[[Category: Leys, D]]
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[[Category: Dunstan MS]]
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[[Category: Hydrolase]]
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[[Category: Leys D]]
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[[Category: Poly adp-ribose]]
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Current revision

The X-ray crystal structure of poly(ADP-ribose) glycohydrolase (PARG) from Thermomonospora curvata

PDB ID 3sih

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