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B6db references: 16511092

type Journal Article
authors Mamaeva, D.V.; Morozovam, E.A.; Nikulinm, A.D.; Revtovichm, S.V.; Nikonovm, S.V.; Garberm, M.B.; Demidkina, T.V.
title Structure of Citrobacter freundiiL-methionine gamma-lyase
journal Acta Crystallograph Sect F Struct Biol Cryst Commun.
sel selected
ui 16511092
year (2005)
volume 61
number 6
pages 546-9
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.
last changed 2008/06/09 17:52

B6db references