4oma

The crystal structure of methionine gamma-lyase from Citrobacter freundii in complex with L-cycloserine pyridoxal-5'-phosphate

spinqualitylabelsall models 4oma, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4oma is a 1 chain structure with sequence from Citrobacter freundii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CL, LCS, PEG, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q84AR1_CITFR Publication Abstract from PubMed MGL catalyzes the gamma-elimination of L-methionine and its derivatives as well as the beta-elimination of L-cysteine and its analogs. These reactions yield alpha-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 MGL-L-cycloserine complex has been solved at 1.6 A resolution. The structure models ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediates interconversion at the stages of external aldimine and ketimine formation. Pre-Steady-State Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.,Kuznetsov NA, Faleev NG, Kuznetsova AA, Morozova EA, Revtovich SV, Anufrieva NV, Nikulin AD, Fedorova OS, Demidkina TV J Biol Chem. 2014 Nov 14. pii: jbc.M114.586511. PMID:25398880 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine gamma-lyase 3D structures

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