3G9D

Crystal structure glycohydrolase

3G9D の概要

• エントリーDOI: 10.2210/pdb3g9d/pdb
• 分子名称: Dinitrogenase reductase activating glucohydrolase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: nitrogenase, drag, adp-ribosylation, posttranslational modification, hydrolase
• 由来する生物種: Azospirillum brasilense
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64982.81

構造登録者

Li, X.-D.,Winkler, F.K. (登録日: 2009-02-13, 公開日: 2009-07-14, 最終更新日: 2023-11-01)

主引用文献

Li, X.-D.,Huergo, L.F.,Gasperina, A.,Pedrosa, F.O.,Merrick, M.,Winkler, F.K.
Crystal Structure of Dinitrogenase Reductase-activating Glycohydrolase (DRAG) Reveals Conservation in the ADP-Ribosylhydrolase Fold and Specific Features in the ADP-Ribose-binding Pocket
J.Mol.Biol., 390:737-746, 2009

PubMed Abstract: Protein-reversible ADP-ribosylation is emerging as an important post-translational modification used to control enzymatic and protein activity in different biological systems. This modification regulates nitrogenase activity in several nitrogen-fixing bacterial species. ADP-ribosylation is catalyzed by ADP-ribosyltransferases and is reversed by ADP-ribosylhydrolases. The structure of the ADP-ribosylhydrolase that acts on Azospirillum brasilense nitrogenase (dinitrogenase reductase-activating glycohydrolase, DraG) has been solved at a resolution of 2.5 A. This bacterial member of the ADP-ribosylhydrolase family acts specifically towards a mono-ADP-ribosylated substrate. The protein shows an all-alpha-helix structure with two magnesium ions located in the active site. Comparison of the DraG structure with orthologues deposited in the Protein Data Bank from Archaea and mammals indicates that the ADP-ribosylhydrolase fold is conserved in all domains of life. Modeling of the binding of the substrate ADP-ribosyl moiety to DraG is in excellent agreement with biochemical data.

PubMed: 19477184
DOI: 10.1016/j.jmb.2009.05.031

実験手法

X-RAY DIFFRACTION (2.5 Å)