Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins.
Mononuclear non-heme ferrous iron dependent oxygenases and oxidases constitute an extended enzyme family that catalyze a wide range of oxidation reactions. The largest known sub-group employs 2-oxoglutarate as a cosubstrate and catalysis by these and closely related enzymes is proposed to proceed via a ferryl intermediate coordinated to the active site via a conserved HXD/E...H motif. Crystallographic studies on the 2-oxoglutarate oxygenases and related enzymes have revealed a common double-stranded beta-helix core fold that supports the residues coordinating the iron. This fold is common to proteins of the cupin and the JmjC transcription factor families. The crystallographic studies on 2-oxoglutarate oxygenases and closely related enzymes are reviewed and compared with other metallo-enzymes/related proteins containing a double-stranded beta-helix fold. Proposals regarding the suitability of the active sites and folds of the 2-oxoglutarate oxygenases to catalyze reactions involving reactive oxidizing species are described.
Clifton
Ian J
IJ
The Oxford Centre for Molecular Sciences and the Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, Oxon OX1 3TA, UK.
McDonough
Michael A
MA
Ehrismann
Dominic
D
Kershaw
Nadia J
NJ
Granatino
Nicolas
N
Schofield
Christopher J
CJ
D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007656:Ketoglutaric Acids / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D007656:Ketoglutaric Acids; C066317:ferryl iron; D007501:Iron; D010105:Oxygenases