3g9d | pdb_00003g9d

Crystal structure glycohydrolase

spinqualitylabelsall models 3g9d, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3g9d is a 2 chain structure with sequence from Atcc 29145. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Gene: draG (ATCC 29145) Activity: [dinitrogen_reductase_hydrolase ADP-ribosyl-[dinitrogen reductase] hydrolase], with EC number 3.2.2.24 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of dinitrogenase reductase-activating glycohydrolase (DraG) reveals conservation in the ADP-ribosylhydrolase fold and specific features in the ADP-ribose-binding pocket.,Li XD, Huergo LF, Gasperina A, Pedrosa FO, Merrick M, Winkler FK J Mol Biol. 2009 Jul 24;390(4):737-46. Epub 2009 May 25. PMID:19477184 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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