2fub

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2fub, resolution 2.30Å

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Crystal structure of urate oxidase at 140 MPa

Overview

We report the three-dimensional structure determined by high-pressure, macromolecular crystallography (HPMX) of a 135-kDa homo-tetrameric enzyme, urate oxidase from Aspergillus flavus complexed with its potent inhibitor, 8-azaxanthin. Urate oxidase crystals are quite sensitive to pressure, as, three-dimensional order is lost at about 180 MPa. A highly complete 2.3 A, resolution data set was collected at 140 MPa, close to the critical, pressure. Crystal structures at atmospheric pressure and at high pressure, were refined in the orthorhombic space group I222 with final, crystallographic R factors 14.1% and 16.1%, respectively. The effect of, pressure on temperature factors, ordered water molecules, hydrogen bond, lengths, contacts, buried surface areas as well as cavity volume was, investigated. Results suggest that the onset of disruption of the, tetrameric assembly by pressure has been captured in the crystalline, state.

About this Structure

2FUB is a Single protein structure of sequence from Aspergillus flavus with AZA and CYS as ligands. Active as Urate oxidase, with EC number 1.7.3.3 Full crystallographic information is available from OCA.

Reference

High pressure macromolecular crystallography: the 140-MPa crystal structure at 2.3 A resolution of urate oxidase, a 135-kDa tetrameric assembly., Colloc'h N, Girard E, Dhaussy AC, Kahn R, Ascone I, Mezouar M, Fourme R, Biochim Biophys Acta. 2006 Mar;1764(3):391-7. Epub 2006 Jan 26. PMID:16478683

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