Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Structural insights into urocanate reductase using room-temperature X-ray crystallography

Aggarwal, Swati LU ; Gurav, Nitisha LU orcid ; Oksanen, Esko LU ; Lindkvist-Petersson, Karin LU and Venskutonytė, Raminta LU (2026) In Acta Crystallographica Section D: Structural Biology 82. p.603-614
Abstract

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... (More)

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.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
active-site anion interactions, room-temperature crystallography, urocanate reductase
in
Acta Crystallographica Section D: Structural Biology
volume
82
pages
12 pages
publisher
John Wiley & Sons Inc.
external identifiers
  • pmid:42083916
  • scopus:105040691551
ISSN
2059-7983
DOI
10.1107/S2059798326003360
language
English
LU publication?
yes
id
de8c843f-c1d4-4869-a0c9-50c9c05e0f1e
date added to LUP
2026-07-03 10:00:25
date last changed
2026-08-14 14:08:20
@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}},
}