title: Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219.
abstract: Class II extradiol-cleaving catecholic dioxygenase, a key enzyme of aromatic compound degradation in bacteria, cleaves the aromatic ring of catechol by adding two O atoms. PheB is one of the class II extradiol-cleaving catecholic dioxygenases and shows a high substrate specificity for catechol derivatives, which have one aromatic ring. In order to reveal the mechanism of the substrate specificity of PheB, PheB has been crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The space group of the obtained crystal was P2(1)2(1)2(1), with unit-cell parameters a = 65.5, b = 119.2, c = 158.7 A. The crystal diffracted to 2.3 A resolution.
authors.affiliation: Department of Material Chemistry, Asahikawa National College of Technology, 2-2-1-6 Shunko-dai, Asahikawa, Hokkaido 071-8142, Japan.
authors.forename: Keisuke
authors.initials: K
authors.lastname: Sugimoto
authors.forename: Kazuki
authors.initials: K
authors.lastname: Matsufuzi
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Ohnuma
authors.forename: Miki
authors.initials: M
authors.lastname: Senda
authors.forename: Masao
authors.initials: M
authors.lastname: Fukuda
authors.forename: Toshiya
authors.initials: T
authors.lastname: Senda
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D050557:Catechol 2,3-Dioxygenase / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D050557:Catechol 2,3-Dioxygenase