5fsv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Trypanosoma brucei macrodomain (crystal form 2)== | |
| + | <StructureSection load='5fsv' size='340' side='right' caption='[[5fsv]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fsv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FSV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FSV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fsu|5fsu]], [[5fsx|5fsx]], [[5fsy|5fsy]], [[5fsz|5fsz]]</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=5fsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fsv OCA], [http://pdbe.org/5fsv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fsv RCSB], [http://www.ebi.ac.uk/pdbsum/5fsv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ADP-ribosylation is a ubiquitous protein modification utilized by both prokaryotes and eukaryotes for several cellular functions, such as DNA repair, proliferation, and cell signaling. Higher eukaryotes, such as humans, utilize various enzymes to reverse the modification and to regulate ADP-ribose dependent signaling. In contrast, some lower eukaryotes, including trypanosomatids, lack many of these enzymes and therefore have a much more simplified ADP-ribose metabolism. Here we identified and characterized ADP-ribose hydrolases from Trypanosoma brucei and Trypanosoma cruzi, which are homologous to human O-acetyl-ADP-ribose deacetylases MacroD1 and MacroD2. The enzymes are capable for hydrolysis of protein linked ADP-ribose and a product of sirtuin-mediated lysine deacetylation, O-acetyl-ADP-ribose. Crystal structures of the trypanosomatid macrodomains revealed a conserved catalytic site with distinct differences to human MacroD1 and MacroD2. | ||
| - | + | Proximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain.,Haikarainen T, Lehtio L Sci Rep. 2016 Apr 11;6:24213. doi: 10.1038/srep24213. PMID:27064071<ref>PMID:27064071</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5fsv" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Haikarainen, T]] | [[Category: Haikarainen, T]] | ||
| + | [[Category: Lehtio, L]] | ||
| + | [[Category: Adp-ribose binding]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Macrodomain]] | ||
Revision as of 18:45, 12 May 2016
Crystal structure of Trypanosoma brucei macrodomain (crystal form 2)
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