3F2M

Urate oxidase complexed with 8-azaxanthine at 150 MPa

3F2M の概要

• エントリーDOI: 10.2210/pdb3f2m/pdb
• 分子名称: Uricase, 8-AZAXANTHINE, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: high pressure, uric acid degradation, tetramer, t-fold domain, peroxisome, purine metabolism, oxidoreductase, hpmx
• 由来する生物種: Aspergillus flavus
• 細胞内の位置: Peroxisome: Q00511
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34359.68

構造登録者

Colloc'h, N.,Girard, E.,Kahn, R.,Fourme, R. (登録日: 2008-10-30, 公開日: 2009-11-10, 最終更新日: 2024-10-30)

主引用文献

Girard, E.,Marchal, S.,Perez, J.,Finet, S.,Kahn, R.,Fourme, R.,Marassio, G.,Dhaussy, A.C.,Prange, T.,Giffard, M.,Dulin, F.,Bonnete, F.,Lange, R.,Abraini, J.H.,Mezouar, M.,Colloc'h, N.
Structure-function perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure.
Biophys.J., 98:2365-2373, 2010

PubMed Abstract: Structure-function relationships in the tetrameric enzyme urate oxidase were investigated using pressure perturbation. As the active sites are located at the interfaces between monomers, enzyme activity is directly related to the integrity of the tetramer. The effect of hydrostatic pressure on the enzyme was investigated by x-ray crystallography, small-angle x-ray scattering, and fluorescence spectroscopy. Enzymatic activity was also measured under pressure and after decompression. A global model, consistent with all measurements, discloses structural and functional details of the pressure-induced dissociation of the tetramer. Before dissociating, the pressurized protein adopts a conformational substate characterized by an expansion of its substrate binding pocket at the expense of a large neighboring hydrophobic cavity. This substate should be adopted by the enzyme during its catalytic mechanism, where the active site has to accommodate larger intermediates and product. The approach, combining several high-pressure techniques, offers a new (to our knowledge) means of exploring structural and functional properties of transient states relevant to protein mechanisms.

PubMed: 20483346
DOI: 10.1016/j.bpj.2010.01.058

実験手法

X-RAY DIFFRACTION (1.8 Å)