7PWN

URATE OXYDASE AZA-XANTHINE COMPLEX AT 1000 BARS (100 MPa) OF ARGON

7PWN の概要

• エントリーDOI: 10.2210/pdb7pwn/pdb
• 関連するPDBエントリー: 6i9x 6i9z 6ia1 6ia3 6ia9 7puf
• 分子名称: Uricase, SODIUM ION, 8-AZAXANTHINE, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, argon, high-pressure
• 由来する生物種: Aspergillus flavus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67561.49

構造登録者

Prange, T.,Colloc'h, N.,Carpentier, P. (登録日: 2021-10-07, 公開日: 2022-02-09, 最終更新日: 2025-07-23)

主引用文献

Prange, T.,Carpentier, P.,Dhaussy, A.C.,van der Linden, P.,Girard, E.,Colloc'h, N.
Comparative study of the effects of high hydrostatic pressure per se and high argon pressure on urate oxidase ligand stabilization.
Acta Crystallogr D Struct Biol, 78:162-173, 2022

PubMed Abstract: The stability of the tetrameric enzyme urate oxidase in complex with excess of 8-azaxanthine was investigated either under high hydrostatic pressure per se or under a high pressure of argon. The active site is located at the interface of two subunits, and the catalytic activity is directly related to the integrity of the tetramer. This study demonstrates that applying pressure to a protein-ligand complex drives the thermodynamic equilibrium towards ligand saturation of the complex, revealing a new binding site. A transient dimeric intermediate that occurs during the pressure-induced dissociation process was characterized under argon pressure and excited substates of the enzyme that occur during the catalytic cycle can be trapped by pressure. Comparison of the different structures under pressure infers an allosteric role of the internal hydrophobic cavity in which argon is bound, since this cavity provides the necessary flexibility for the active site to function.

PubMed: 35102882
DOI: 10.1107/S2059798321012134

実験手法

X-RAY DIFFRACTION (1.64 Å)