5K30
Crystal structure of methionine gamma-lyase from Citrobacter freundii modified by S-Ethyl-L-cysteine sulfoxide
Summary for 5K30
| Entry DOI | 10.2210/pdb5k30/pdb |
| Related | 2RFV |
| Descriptor | Methionine gamma-lyase, PYRIDOXAL-5'-PHOSPHATE, PENTAETHYLENE GLYCOL, ... (7 entities in total) |
| Functional Keywords | methionine gamma-lyase, lyase |
| Biological source | Citrobacter freundii |
| Total number of polymer chains | 1 |
| Total formula weight | 44131.18 |
| Authors | Revtovich, S.V.,Nikulin, A.D.,Morozova, E.A.,Demidkina, T.V. (deposition date: 2016-05-19, release date: 2017-07-12, Last modification date: 2024-01-10) |
| Primary citation | Revtovich, S.,Morozova, E.,Kulikova, V.,Koval, V.,Anufrieva, N.,Nikulin, A.,Demidkina, T. Sulfoxides of sulfur-containing amino acids are suicide substrates of Citrobacter freundii methionine gamma-lyase. Structural bases of the enzyme inactivation. Biochimie, 168:190-197, 2020 Cited by PubMed Abstract: Interactions of Citrobacter freundii methionine γ-lyase (MGL) with sulfoxides of typical substrates were investigated. It was found that sulfoxides are suicide substrates of the enzyme. The products of the β- and γ-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 1.46 Å and 1.59 Å 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 β-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. PubMed: 31711941DOI: 10.1016/j.biochi.2019.11.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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