5fsy | pdb_00005fsy

Crystal structure of Trypanosoma brucei macrodomain in complex with ADP-ribose

spinqualitylabelsall models 5fsy, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fsy is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AR6 Related: 5fsu, 5fsv, 5fsx, 5fsz Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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