Expression, purification, crystallization and initial crystallographic characterization of the p-hydroxybenzoate hydroxylase from Corynebacterium glutamicum

Soo Young Kwon, Beom Sik Kang, Ghyung Hwa Kim, Kyung Jin Kim

Research output: Contribution to journalArticlepeer-review

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Abstract

p-Hydroxybenzoate hydroxylase (PHBH) is an FAD-dependent mono-oxygenase 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 NaH2PO4 and K2HPO4 as precipitants. X-ray diffraction data were collected to a maximum resolution of 2.5 Å on a synchrotron beamline. The crystal belongs to the hexagonal space group P6322, with unit-cell parameters a = b = 94.72, c = 359.68 Å, γ = 120°. The asymmetric unit contains two molecules, corresponding to a packing density of 2.65 Å3 Da-1. The structure was solved by molecular replacement. Structure refinement is in progress.

Original languageEnglish
Pages (from-to)944-946
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number11
DOIs
StatePublished - 2007

Keywords

  • Corynebacterium glutamicum
  • FAD-dependent monooxygenases
  • p-hydroxybenzoate hydroxylase

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