6I9X

urate oxidase under 35 bar of argon

Summary for 6I9X

• Entry DOI: 10.2210/pdb6i9x/pdb
• Related: 1R51 1XT4 2IBA 2IC0 2ICQ 3PLM 4OP6 5FRC
• Descriptor: Uricase, 8-AZAXANTHINE, ARGON, ... (5 entities in total)
• Functional Keywords: aspergillus flavus, homotetramer, purine metabolism, argon, high pressure, oxidoreductase
• Biological source: Aspergillus flavus
• Total number of polymer chains: 1
• Total formula weight: 34399.63

Authors

Prange, T.,Colloc'h, N. (deposition date: 2018-11-26, release date: 2019-12-18, Last modification date: 2025-07-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)