1Y4I

Crystal structure of Citrobacter Freundii L-methionine-lyase

Summary for 1Y4I

Entry DOI	10.2210/pdb1y4i/pdb
Descriptor	methionine gamma-lyase, SULFATE ION (3 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	43317.07
Authors	Revtovich, S.V.,Mamaeva, D.V.,Morozova, E.A.,Nikulin, A.D.,Nikonov, S.V.,Garber, M.B.,Demidkina, T.V. (deposition date: 2004-12-01, release date: 2005-06-14, Last modification date: 2023-11-15)
Primary citation	Mamaeva, D.V.,Morozova, E.A.,Nikulin, A.D.,Revtovich, S.V.,Nikonov, S.V.,Garber, M.B.,Demidkina, T.V. Structure of Citrobacter freundii L-methionine gamma-lyase. Acta Crystallogr.,Sect.F, 61:546-549, 2005 Cited by PubMed Abstract: L-Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate (PLP) dependent enzyme that catalyzes gamma-elimination of L-methionine. The crystal structure of MGL from Citrobacter freundii has been determined at 1.9 A resolution. The spatial fold of the protein is similar to those of MGLs from Pseudomonas putida and Trichomonas vaginalis. The comparison of these structures revealed that there are differences in PLP-binding residues and positioning of the surrounding flexible loops. PubMed: 16511092 DOI: 10.1107/S1744309105015447 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation