5DX5: Crystal Structure Of Methionine Gamma-lyase From Clostridium Sporogenes

Citation:
Abstract
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.
PDB ID: 5DX5Download
MMDB ID: 135495
PDB Deposition Date: 2015/9/23
Updated in MMDB: 2016/01
Experimental Method:
x-ray diffraction
Resolution: 2.37  Å
Source Organism:
Similar Structures:
Biological Unit for 5DX5: tetrameric; determined by author and by software (PISA)
Molecular Components in 5DX5
Label Count Molecule
Proteins (4 molecules)
4
Methionine Gamma-lyase
Molecule annotation
Chemicals (10 molecules)
1
4
2
4
3
2
* Click molecule labels to explore molecular sequence information.

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