4OMA
The crystal structure of methionine gamma-lyase from Citrobacter freundii in complex with L-cycloserine pyridoxal-5'-phosphate
Summary for 4OMA
| Entry DOI | 10.2210/pdb4oma/pdb |
| Related | 1D7U 2DAA 2RFV 4HF8 |
| Descriptor | methionine gamma-lyase, [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate, TRIETHYLENE GLYCOL, ... (6 entities in total) |
| Functional Keywords | aminotransferase class i and ii, methionine, lyase |
| Biological source | Citrobacter freundii |
| Total number of polymer chains | 1 |
| Total formula weight | 43816.06 |
| Authors | Revtovich, S.V.,Nikulin, A.D.,Morozova, E.A.,Demidkina, T.V. (deposition date: 2014-01-27, release date: 2014-11-26, Last modification date: 2023-09-20) |
| Primary citation | Kuznetsov, N.A.,Faleev, N.G.,Kuznetsova, A.A.,Morozova, E.A.,Revtovich, S.V.,Anufrieva, N.V.,Nikulin, A.D.,Fedorova, O.S.,Demidkina, T.V. Pre-steady-state Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors. J.Biol.Chem., 290:671-681, 2015 Cited by PubMed Abstract: Methionine γ-lyase (MGL) catalyzes the γ-elimination of l-methionine and its derivatives as well as the β-elimination of l-cysteine and its analogs. These reactions yield α-keto acids and thiols. The mechanism of chemical conversion of amino acids includes numerous reaction intermediates. The detailed analysis of MGL interaction with glycine, l-alanine, l-norvaline, and l-cycloserine was performed by pre-steady-state stopped-flow kinetics. The structure of side chains of the amino acids is important both for their binding with enzyme and for the stability of the external aldimine and ketimine intermediates. X-ray structure of the MGL·l-cycloserine complex has been solved at 1.6 Å resolution. The structure models the ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediate interconversion at the stages of external aldimine and ketimine formation. PubMed: 25398880DOI: 10.1074/jbc.M114.586511 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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