title: Expression, purification, crystallization and initial crystallographic characterization of the p-hydroxybenzoate hydroxylase from Corynebacterium glutamicum.
abstract: p-Hydroxybenzoate hydroxylase (PHBH) is an FAD-dependent monooxygenase that catalyzes the hydroxylation of p-hydroxybenzoate (pOHB) to 3,4-dihydroxybenzoate in an NADPH-dependent reaction and plays an important role in the biodegradation of aromatic compounds. PHBH from Corynebacterium glutamicum was crystallized using the hanging-drop vapour-diffusion method in the presence of NaH(2)PO(4) and K(2)HPO(4) as precipitants. X-ray diffraction data were collected to a maximum resolution of 2.5 A on a synchrotron beamline. The crystal belongs to the hexagonal space group P6(3)22, with unit-cell parameters a = b = 94.72, c = 359.68 A, gamma = 120 degrees . The asymmetric unit contains two molecules, corresponding to a packing density of 2.65 A(3) Da(-1). The structure was solved by molecular replacement. Structure refinement is in progress.
authors.affiliation: Beamline Division, Pohang Accelerator Laboratory, Pohang, Kyungbuk 790-784, South Korea.
authors.forename: Soo Young
authors.initials: SY
authors.lastname: Kwon
authors.forename: Beom Sik
authors.initials: BS
authors.lastname: Kang
authors.forename: Ghyung Hwa
authors.initials: GH
authors.lastname: Kim
authors.forename: Kyung Jin
authors.initials: KJ
authors.lastname: Kim
mesh_terms: D015109:4-Hydroxybenzoate-3-Monooxygenase / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D048230:Corynebacterium glutamicum / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray
chemical_list: D015109:4-Hydroxybenzoate-3-Monooxygenase