6hh5: Difference between revisions
New page: '''Unreleased structure''' The entry 6hh5 is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-HPM== | |||
<StructureSection load='6hh5' size='340' side='right' caption='[[6hh5]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6hh5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Latch Latch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HH5 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A3R:Adenosine+Diphosphate+(Hydroxymethyl)pyrrolidine+monoalcohol'>A3R</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADPRHL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7897 LATCH])</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=6hh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hh5 OCA], [http://pdbe.org/6hh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hh5 RCSB], [http://www.ebi.ac.uk/pdbsum/6hh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hh5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Protein ADP-ribosylation is a highly dynamic post-translational modification. The rapid turnover is achieved, among others, by ADP-(ribosyl)hydrolases (ARHs), an ancient family of enzymes that reverses this modification. Recently ARHs came into focus due to their role as regulators of cellular stresses and tumor suppressors. Here we present a comprehensive structural analysis of the enzymatically active family members ARH1 and ARH3. These two enzymes have very distinct substrate requirements. Our data show that binding of the adenosine ribose moiety is highly diverged between the two enzymes, whereas the active sites harboring the distal ribose closely resemble each other. Despite this apparent similarity, we elucidate the structural basis for the selective inhibition of ARH3 by the ADP-ribose analogues ADP-HPD and arginine-ADP-ribose. Together, our biochemical and structural work provides important insights into the mode of enzyme-ligand interaction, helps to understand differences in their catalytic behavior, and provides useful tools for targeted drug design. | |||
(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.,Rack JGM, Ariza A, Drown BS, Henfrey C, Bartlett E, Shirai T, Hergenrother PJ, Ahel I Cell Chem Biol. 2018 Nov 16. pii: S2451-9456(18)30389-1. doi:, 10.1016/j.chembiol.2018.11.001. PMID:30472116<ref>PMID:30472116</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6hh5" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Latch]] | |||
[[Category: Ariza, A]] | |||
[[Category: Adp-hpm]] | |||
[[Category: Adp-ribose]] | |||
[[Category: Adp-ribosylation]] | |||
[[Category: Adp-ribosylhydrolase like 2]] | |||
[[Category: Adprhl2]] | |||
[[Category: Hydrolase]] | |||
Latest revision as of 10:08, 5 December 2018
ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-HPMADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with ADP-HPM
Structural highlights
Publication Abstract from PubMedProtein ADP-ribosylation is a highly dynamic post-translational modification. The rapid turnover is achieved, among others, by ADP-(ribosyl)hydrolases (ARHs), an ancient family of enzymes that reverses this modification. Recently ARHs came into focus due to their role as regulators of cellular stresses and tumor suppressors. Here we present a comprehensive structural analysis of the enzymatically active family members ARH1 and ARH3. These two enzymes have very distinct substrate requirements. Our data show that binding of the adenosine ribose moiety is highly diverged between the two enzymes, whereas the active sites harboring the distal ribose closely resemble each other. Despite this apparent similarity, we elucidate the structural basis for the selective inhibition of ARH3 by the ADP-ribose analogues ADP-HPD and arginine-ADP-ribose. Together, our biochemical and structural work provides important insights into the mode of enzyme-ligand interaction, helps to understand differences in their catalytic behavior, and provides useful tools for targeted drug design. (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.,Rack JGM, Ariza A, Drown BS, Henfrey C, Bartlett E, Shirai T, Hergenrother PJ, Ahel I Cell Chem Biol. 2018 Nov 16. pii: S2451-9456(18)30389-1. doi:, 10.1016/j.chembiol.2018.11.001. PMID:30472116[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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