Structure of the cystathionine γ-synthase MetB from Mycobacterium ulcerans
Author Information
Author(s): Clifton Matthew C., Abendroth Jan, Edwards Thomas E., Leibly David J., Gillespie Angela K., Ferrell Micah, Dieterich Shellie H., Exley Ilyssa, Staker Bart L., Myler Peter J., deVan Voorhis Wesley C., Stewart Lance J.
Primary Institution: Seattle Structural Genomics Center for Infectious Disease
Hypothesis
The study aims to present the crystal structure of cystathionine γ-synthase from Mycobacterium ulcerans.
Conclusion
The study reports two high-resolution structures of MetB, one bound to PLP and another to PLP and HEPES, marking the first structure reported from M. ulcerans.
Supporting Evidence
- The crystal structure of CGS from M. ulcerans is presented at 1.9 Å resolution.
- This is the first structure ever reported from the pathogen M. ulcerans.
- MetB forms a homotetramer, similar to other CGS enzymes.
- HEPES molecule acts as a pseudo-ligand in the active site.
Takeaway
Scientists figured out the shape of an important enzyme from a germ that causes skin infections, which could help in making new medicines.
Methodology
The study involved protein expression, purification, crystallization, and X-ray data collection to determine the structure of MetB.
Digital Object Identifier (DOI)
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