5FSU

Crystal structure of Trypanosoma brucei macrodomain (crystal form 1)

Summary for 5FSU

• Entry DOI: 10.2210/pdb5fsu/pdb
• Related: 5FSV 5FSX 5FSY 5FSZ
• Descriptor: MACRODOMAIN (2 entities in total)
• Functional Keywords: macrodomain, hydrolase, adp-ribose binding
• Biological source: TRYPANOSOMA BRUCEI
• Total number of polymer chains: 2
• Total formula weight: 58351.11

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

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: 27064071
DOI: 10.1038/SREP24213

Experimental method

X-RAY DIFFRACTION (1.95 Å)