Crystallization and preliminary X-ray crystallographic analysis of hydroquinone dioxygenase from Sphingomonas sp. TTNP3.

ABSTRACT: Hydroquinone dioxygenase (HQDO), a novel Fe(II) ring-fission dioxygenase from Sphingomonas sp. strain TTNP3 which oxidizes a wide range of hydroquinones to the corresponding 4-hydroxymuconic semialdehydes, has been crystallized. The enzyme is an ?(2)?(2) heterotetramer constituted of two subunits of 19 and 38?kDa. Diffraction-quality crystals of HQDO were obtained using the sitting-drop vapour-diffusion method at 277?K from a solution consisting of 16% PEG 4000, 0.3?M MgCl(2), 0.1?M Tris pH 8.5. The crystals belonged to the monoclinic space group P2(1), with unit-cell parameters a = 88.4, b = 125.4, c = 90.8?Å, ? = 105.3°. The asymmetric unit contained two heterotetramers, i.e. four copies of each of the two different subunits related by noncrystallographic 222 symmetry. A complete data set extending to a maximum resolution of 2.5?Å was collected at 100?K using a wavelength of 0.980?Å.

SUBMITTER: Da Vela S 

PROVIDER: S-EPMC3374519 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature