5LSQ
Ethylene Forming Enzyme from Pseudomonas syringae pv. phaseolicola - I222 crystal form
Summary for 5LSQ
| Entry DOI | 10.2210/pdb5lsq/pdb |
| Descriptor | Ethylene 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 syringae |
| Total number of polymer chains | 1 |
| Total formula weight | 41256.78 |
| Authors | Zhang, Z.,McDonough, M.A.,Schofield, C.J. (deposition date: 2016-09-05, release date: 2017-04-19, Last modification date: 2024-05-08) |
| 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 Cited by 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: 28420789DOI: 10.1073/pnas.1617760114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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