Structural highlights
Function
Q84AR1_CITFR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of Citrobacter freundii L-methionine gamma-lyase.,Mamaeva DV, Morozova EA, Nikulin AD, Revtovich SV, Nikonov SV, Garber MB, Demidkina TV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt, 6):546-9. Epub 2005 Jun 1. PMID:16511092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mamaeva DV, Morozova EA, Nikulin AD, Revtovich SV, Nikonov SV, Garber MB, Demidkina TV. Structure of Citrobacter freundii L-methionine gamma-lyase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jun 1;61(Pt, 6):546-9. Epub 2005 Jun 1. PMID:16511092 doi:10.1107/S1744309105015447
