View source for 5fsx


==Crystal structure of Trypanosoma brucei macrodomain in complex with ADP==
<StructureSection load='5fsx' size='340' side='right'caption='[[5fsx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fsx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FSX 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]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5fsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fsx OCA], [https://pdbe.org/5fsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fsx RCSB], [https://www.ebi.ac.uk/pdbsum/5fsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fsx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C9ZP98_TRYB9 C9ZP98_TRYB9] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fsx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trypanosoma brucei]]
[[Category: Haikarainen T]]
[[Category: Lehtio L]]