9TK7

Cryogenic temperature structure of urocanate reductase in complex with imidazole propionate and sulfate

9TK7 の概要

• エントリーDOI: 10.2210/pdb9tk7/pdb
• 分子名称: Urocanate reductase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: urocanate reductase, imidazole propionate, oxidoreductase
• 由来する生物種: Shewanella oneidensis MR-1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51769.99

構造登録者

Aggarwal, S.,Gurav, N.,Oksanen, E.,Lindkvist-Petersson, K.,Venskutonyte, R. (登録日: 2025-12-08, 公開日: 2026-05-20, 最終更新日: 2026-06-10)

主引用文献

Aggarwal, S.,Gurav, N.,Oksanen, E.,Lindkvist-Petersson, K.,Venskutonyte, R.
Structural insights into urocanate reductase using room-temperature X-ray crystallography.
Acta Crystallogr D Struct Biol, 82:603-614, 2026

PubMed 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 distinct conformational states.

PubMed: 42083916
DOI: 10.1107/S2059798326003360

実験手法

X-RAY DIFFRACTION (1.5 Å)