Crystal structure of Trypanosoma brucei macrodomain in complex with ADPCrystal structure of Trypanosoma brucei macrodomain in complex with ADP

Structural highlights

5fsx is a 2 chain structure with sequence from Trypanosoma brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C9ZP98_TRYB9

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Haikarainen T, Lehtio L. Proximal ADP-ribose Hydrolysis in Trypanosomatids is Catalyzed by a Macrodomain. Sci Rep. 2016 Apr 11;6:24213. doi: 10.1038/srep24213. PMID:27064071 doi:http://dx.doi.org/10.1038/srep24213

5fsx, resolution 2.00Å

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