Structure of Citrobacter freundii L-methionine gamma-lyase

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
D V MamaevaT V Demidkina

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.

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Citations

Oct 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Dan SatoShigeharu Harada
Aug 6, 2008·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Dan SatoTomoyoshi Nozaki
Aug 9, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Jiang YinMichael N G James
Apr 18, 2006·Biochemistry. Biokhimii︠a︡·I V ManukhovG B Zavilgelsky
Jan 12, 2016·Acta Crystallographica. Section F, Structural Biology Communications·Svetlana RevtovichTatyana Demidkina
Jan 15, 2015·Biochimica Et Biophysica Acta·Natalya V AnufrievaTatyana V Demidkina
Sep 25, 2014·BioMed Research International·Bhupender SharmaShamsher S Kanwar
Mar 3, 2010·The Journal of Biological Chemistry·Dusan GoranovicHrvoje Petkovic
Nov 16, 2014·The Journal of Biological Chemistry·Nikita A KuznetsovTatyana V Demidkina

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