@article{de8c843f-c1d4-4869-a0c9-50c9c05e0f1e,
  abstract     = {{<p>Urocanate reductase (UrdA) is a bacterial enzyme that converts urocanic acid to imidazole propionate. Its catalytic residue Arg411 undergoes a large conformational change in the substrate-bound versus product-bound states. In contrast to previously studied cryo-conditions, the room-temperature X-ray data of UrdA presented here show that the occupancy distribution of Arg411 is affected by crystal cryocooling. We further provide evidence that a phosphate ion stabilizes the substrate complex and can bias the conformation of Arg411. Both room-temperature and cryogenic X-ray datasets were essential to elucidate the dynamic nature of the UrdA active site, highlighting the importance of collecting data at both temperatures, as each may reveal distinct conformational states.</p>}},
  author       = {{Aggarwal, Swati and Gurav, Nitisha and Oksanen, Esko and Lindkvist-Petersson, Karin and Venskutonytė, Raminta}},
  issn         = {{2059-7983}},
  keywords     = {{active-site anion interactions; room-temperature crystallography; urocanate reductase}},
  language     = {{eng}},
  pages        = {{603--614}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Acta Crystallographica Section D: Structural Biology}},
  title        = {{Structural insights into urocanate reductase using room-temperature X-ray crystallography}},
  url          = {{http://dx.doi.org/10.1107/S2059798326003360}},
  doi          = {{10.1107/S2059798326003360}},
  volume       = {{82}},
  year         = {{2026}},
}