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==Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase==
==Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase==
<StructureSection load='3uek' size='340' side='right' caption='[[3uek]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3uek' size='340' side='right'caption='[[3uek]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3uek]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UEK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3uek]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UEK FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uel|3uel]]</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]] 1.95&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Parg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=3uek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uek OCA], [https://pdbe.org/3uek PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uek RCSB], [https://www.ebi.ac.uk/pdbsum/3uek PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uek ProSAT]</span></td></tr>
<tr><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>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3uek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uek OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uek RCSB], [http://www.ebi.ac.uk/pdbsum/3uek PDBsum]</span></td></tr>
== Function ==
<table>
[https://www.uniprot.org/uniprot/PARG_RAT PARG_RAT] Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Reversible post-translational modification by poly(ADP-ribose) (PAR) regulates chromatin structure, DNA repair and cell fate in response to genotoxic stress. PAR glycohydrolase (PARG) removes PAR chains from poly ADP-ribosylated proteins to restore protein function and release oligo(ADP-ribose) chains to signal damage. Here we report crystal structures of mammalian PARG and its complex with a substrate mimic that reveal an open substrate-binding site and a unique 'tyrosine clasp' enabling endoglycosidic cleavage of branched PAR chains.
 
Structure of mammalian poly(ADP-ribose) glycohydrolase reveals a flexible tyrosine clasp as a substrate-binding element.,Kim IK, Kiefer JR, Ho CM, Stegeman RA, Classen S, Tainer JA, Ellenberger T Nat Struct Mol Biol. 2012 May 20;19(6):653-6. doi: 10.1038/nsmb.2305. PMID:22609859<ref>PMID:22609859</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Poly(ADP-ribose) glycohydrolase 3D structures|Poly(ADP-ribose) glycohydrolase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Classen, S.]]
[[Category: Classen S]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger T]]
[[Category: Kiefer, J R.]]
[[Category: Kiefer JR]]
[[Category: Kim, I K.]]
[[Category: Kim IK]]
[[Category: Stegemann, R A.]]
[[Category: Stegemann RA]]
[[Category: Tainer, J A.]]
[[Category: Tainer JA]]
[[Category: Hydrolase]]
[[Category: Macrodomain]]
[[Category: Mammalian parg]]

Latest revision as of 13:21, 1 March 2024

Crystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolaseCrystal structure of the catalytic domain of rat poly (ADP-ribose) glycohydrolase

Structural highlights

3uek is a 1 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PARG_RAT Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. PARG acts both as an endo- and exoglycosidase, releasing PAR of different length as well as ADP-ribose monomers. Required for retinoid acid-dependent gene transactivation, probably by dePARsylating histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters (By similarity).

See Also

3uek, resolution 1.95Å

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