5FSV
Crystal structure of Trypanosoma brucei macrodomain (crystal form 2)
Summary for 5FSV
| Entry DOI | 10.2210/pdb5fsv/pdb |
| Related | 5FSU 5FSX 5FSY 5FSZ |
| Descriptor | MACRODOMAIN, GLYCEROL (3 entities in total) |
| Functional Keywords | macrodomain, hydrolase, adp-ribose binding |
| Biological source | TRYPANOSOMA BRUCEI |
| Total number of polymer chains | 1 |
| Total formula weight | 29359.74 |
| Authors | Haikarainen, T.,Lehtio, L. (deposition date: 2016-01-08, release date: 2016-04-20, Last modification date: 2024-01-10) |
| Primary citation | Haikarainen, T.,Lehtio, L. Proximal Adp-Ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain. Sci.Rep., 6:24213-, 2016 Cited by PubMed Abstract: 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. PubMed: 27064071DOI: 10.1038/SREP24213 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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