3JW9
Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with S-ethyl-cysteine
Summary for 3JW9
| Entry DOI | 10.2210/pdb3jw9/pdb |
| Related | 1E5E 1UKJ 1Y4I 2O7C 2RFV 3JWA 3JWB |
| Descriptor | Methionine gamma-lyase, S-ethyl-L-cysteine, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | pyridoxal-5'-phosphate, plp-dependent enzyme, lyase |
| Biological source | Citrobacter freundii |
| Total number of polymer chains | 1 |
| Total formula weight | 43420.25 |
| Authors | Revtovish, S.V.,Nikulin, A.D.,Morozova, E.A.,Demidkina, T.V. (deposition date: 2009-09-18, release date: 2010-09-08, Last modification date: 2023-11-22) |
| Primary citation | Revtovich, S.V.,Morozova, E.A.,Khurs, E.N.,Zakomirdina, L.N.,Nikulin, A.D.,Demidkina, T.V.,Khomutov, R.M. Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates. Biochemistry Mosc., 76:564-570, 2011 Cited by PubMed Abstract: Crystal structures of Citrobacter freundii methionine γ-lyase complexes with the substrates of γ- (L-1-amino-3-methylthiopropylphosphinic acid) and β- (S-ethyl-L-cysteine) elimination reactions and the competitive inhibitor L-norleucine have been determined at 1.45, 1.8, and 1.63 Å resolution, respectively. All three amino acids occupy the active site of the enzyme but do not form a covalent bond with pyridoxal 5'-phosphate. Hydrophobic interactions between the active site residues and the side groups of the substrates and the inhibitor are supposed to cause noncovalent binding. Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrates and the inhibitor. The hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acids. PubMed: 21639836DOI: 10.1134/S0006297911050063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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