5k30

Crystal structure of methionine gamma-lyase from Citrobacter freundii modified by S-Ethyl-L-cysteine sulfoxide

spinqualitylabelsall models 5k30, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5k30 is a 1 chain structure with sequence from Citrobacter freundii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.59Å Ligands: 1PE, PEG, PGE, PLP, SCS, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0A5P8W7_CITFR Publication Abstract from PubMed Interactions of Citrobacter freundii methionine gamma-lyase (MGL) with sulfoxides of typical substrates were investigated. It was found that sulfoxides are suicide substrates of the enzyme. The products of the beta- and gamma-elimination reactions of sulfoxides, thiosulfinates, oxidize three cysteine residues of the enzyme. Three-dimensional structures of MGL inactivated by dimethyl thiosulfinate and diethyl thiosulfinate were determined at 1.46A and 1.59A resolution. Analysis of the structures identified SH groups oxidized by thiosulfinates and revealed the structural bases of MGL inactivation. The extent of inactivation of MGL in the catalysis of the beta-elimination reaction depends on the length of the <<tail>> at oxidized Cys115. Oxidation of Cys115 results in MGL incapable to catalyze the stage of methyl mercaptan elimination of the physiological reaction. Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine gamma-lyase. Structural bases of the enzyme inactivation.,Revtovich S, Morozova E, Kulikova V, Koval V, Anufrieva N, Nikulin A, Demidkina T Biochimie. 2020 Jan;168:190-197. doi: 10.1016/j.biochi.2019.11.004. Epub 2019 Nov, 9. PMID:31711941 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methionine gamma-lyase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA