5MOF

Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - I222 crystal form in complex with manganese and 2-oxoglutarate

Summary for 5MOF

• Entry DOI: 10.2210/pdb5mof/pdb
• Descriptor: 2-oxoglutarate-dependent ethylene/succinate-forming enzyme, MANGANESE (II) ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: 2-oxoglutarate and ferrous iron dependent oxygenase, ethylene forming, double stranded beta helix, oxidoreductase
• Biological source: Pseudomonas savastanoi pv. phaseolicola
• Total number of polymer chains: 1
• Total formula weight: 41321.58

Authors

McDonough, M.A.,Zhang, Z.,Schofield, C.J. (deposition date: 2016-12-14, release date: 2017-04-19, Last modification date: 2024-01-17)

Primary citation

Zhang, Z.,Smart, T.J.,Choi, H.,Hardy, F.,Lohans, C.T.,Abboud, M.I.,Richardson, M.S.W.,Paton, R.S.,McDonough, M.A.,Schofield, C.J.
Structural and stereoelectronic insights into oxygenase-catalyzed formation of ethylene from 2-oxoglutarate.
Proc. Natl. Acad. Sci. U.S.A., 114:4667-4672, 2017

PubMed Abstract: Ethylene is important in industry and biological signaling. In plants, ethylene is produced by oxidation of 1-aminocyclopropane-1-carboxylic acid, as catalyzed by 1-aminocyclopropane-1-carboxylic acid oxidase. Bacteria catalyze ethylene production, but via the four-electron oxidation of 2-oxoglutarate to give ethylene in an arginine-dependent reaction. Crystallographic and biochemical studies on the ethylene-forming enzyme reveal a branched mechanism. In one branch, an apparently typical 2-oxoglutarate oxygenase reaction to give succinate, carbon dioxide, and sometimes pyrroline-5-carboxylate occurs. Alternatively, Grob-type oxidative fragmentation of a 2-oxoglutarate-derived intermediate occurs to give ethylene and carbon dioxide. Crystallographic and quantum chemical studies reveal that fragmentation to give ethylene is promoted by binding of l-arginine in a nonoxidized conformation and of 2-oxoglutarate in an unprecedented high-energy conformation that favors ethylene, relative to succinate formation.

PubMed: 28420789
DOI: 10.1073/pnas.1617760114

Experimental method

X-RAY DIFFRACTION (1.45 Å)