3G9D

Crystal structure glycohydrolase

Summary for 3G9D

• Entry DOI: 10.2210/pdb3g9d/pdb
• Descriptor: Dinitrogenase reductase activating glucohydrolase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: nitrogenase, drag, adp-ribosylation, posttranslational modification, hydrolase
• Biological source: Azospirillum brasilense
• Total number of polymer chains: 2
• Total formula weight: 64982.81

Authors

Li, X.-D.,Winkler, F.K. (deposition date: 2009-02-13, release date: 2009-07-14, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)