Raminta Venskutonytė, PhD

Urocanate reductase is a bacterial enzyme present in certain members of the human gut microbiota. It catalyzes the production of imidazole propionate, a metabolite that has been linked to type 2 diabetes and other diseases.

We applied X-ray crystallography to gain insight into the enzymatic mechanism and active-site dynamics. By combining cryogenic and room-temperature data collection, we reveal distinct conformational states of the enzyme, highlight the dynamics of key catalytic residues, and uncover the influence of small modulating molecules in the active site.

Beyond the biological findings, this study also illustrates the advantages and limitations of crystallographic data collection at different temperatures.