5DX5
Crystal structure of methionine gamma-lyase from Clostridium sporogenes
Summary for 5DX5
| Entry DOI | 10.2210/pdb5dx5/pdb |
| Descriptor | Methionine gamma-lyase, PYRIDOXAL-5'-PHOSPHATE, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | methionine gamma-lyase, lyase, clostridium sporogenes |
| Biological source | Clostridium sporogenes |
| Total number of polymer chains | 2 |
| Total formula weight | 87747.63 |
| Authors | Revtovich, S.V.,Nikulin, A.D.,Morozova, E.A.,Anufrieva, N.V.,Demidkina, T.V. (deposition date: 2015-09-23, release date: 2016-01-13, Last modification date: 2024-01-10) |
| Primary citation | Revtovich, S.,Anufrieva, N.,Morozova, E.,Kulikova, V.,Nikulin, A.,Demidkina, T. Structure of methionine gamma-lyase from Clostridium sporogenes. Acta Crystallogr.,Sect.F, 72:65-71, 2016 Cited by PubMed Abstract: Methionine γ-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the γ-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 Å 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. PubMed: 26750487DOI: 10.1107/S2053230X15023869 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
Download full validation report
