AI Article Synopsis
- Methionine γ-lyase (MGL) is an enzyme that plays a role in breaking down L-methionine and is being researched for potential cancer therapies and treatments for certain anaerobic pathogens.
- The crystal structure of MGL from Clostridium sporogenes has been resolved at a high resolution of 2.37 Å, revealing important details about its architecture.
- A comparison with similar enzymes from other organisms highlighted differences in two flexible areas at the N- and C-terminal domains that are crucial for the enzyme's active site.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4708053 | PMC |
| http://dx.doi.org/10.1107/S2053230X15023869 | DOI Listing |
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