Structure of Citrobacter freundii L-methionine gamma-lyase

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 Ps...

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Veröffentlicht in:	Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-06, Vol.61 (Pt 6), p.546-549
Hauptverfasser:	Mamaeva, D V, Morozova, E A, Nikulin, A D, Revtovich, S V, Nikonov, S V, Garber, M B, Demidkina, T V
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Binding Sites Carbon-Sulfur Lyases - chemistry Citrobacter freundii - enzymology Crystallography, X-Ray Molecular Structure Protein Structure Communications Protein Structure, Secondary
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Beschreibung
Zusammenfassung:	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.
ISSN:	1744-3091 1744-3091
DOI:	10.1107/S1744309105015447