2fub
Crystal structure of urate oxidase at 140 MPa
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| , resolution 2.30Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Urate oxidase, with EC number 1.7.3.3 | ||||||
| Related: | 1R51
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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 StructureAbout this Structure
2FUB is a Single protein structure of sequence from Aspergillus flavus. Full crystallographic information is available from OCA.
ReferenceReference
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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