5dx5

Crystal structure of methionine gamma-lyase from Clostridium sporogenesCrystal structure of methionine gamma-lyase from Clostridium sporogenes

Structural highlights 5dx5 is a 2 chain structure with sequence from Clostridium sporogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.37Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function J7TA22_CLOS1 Publication Abstract from PubMed Methionine gamma-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the gamma-elimination reaction of L-methionine. The enzyme is a promising target for therapeutic intervention in some anaerobic pathogens and has attracted interest as a potential cancer treatment. The crystal structure of MGL from Clostridium sporogenes has been determined at 2.37 A resolution. The fold of the protein is similar to those of homologous enzymes from Citrobacter freundii, Entamoeba histolytica, Pseudomonas putida and Trichomonas vaginalis. A comparison of these structures revealed differences in the conformation of two flexible regions of the N- and C-terminal domains involved in the active-site architecture. Structure of methionine gamma-lyase from Clostridium sporogenes.,Revtovich S, Anufrieva N, Morozova E, Kulikova V, Nikulin A, Demidkina T Acta Crystallogr F Struct Biol Commun. 2016 Jan 1;72(Pt 1):65-71. doi:, 10.1107/S2053230X15023869. Epub 2016 Jan 1. PMID:26750487 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine gamma-lyase 3D structures

spinqualitylabelsall models 5dx5, resolution 2.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image