5FSX

Crystal structure of Trypanosoma brucei macrodomain in complex with ADP

5FSX の概要

• エントリーDOI: 10.2210/pdb5fsx/pdb
• 関連するPDBエントリー: 5FSU 5FSV 5FSY 5FSZ
• 分子名称: MACRODOMAIN, ADENOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: macrodomain, hydrolase, adp-ribose binding
• 由来する生物種: TRYPANOSOMA BRUCEI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59297.61

構造登録者

Haikarainen, T.,Lehtio, L. (登録日: 2016-01-08, 公開日: 2016-04-20, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)