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Title: Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219

Abstract

PheB, an extradiol-cleaving catecholic dioxygenase, was crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystal belongs to the orthorhombic system, space group P2{sub 1}2{sub 1}2{sub 1}, and diffracts to 2.3 Å resolution. 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{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 65.5, b = 119.2, c = 158.7 Å. The crystal diffracted to 2.3 Å resolution.

Authors:
; ;  [1];  [2];  [3];  [4]
  1. Department of Material Chemistry, Asahikawa National College of Technology, 2-2-1-6 Shunko-dai, Asahikawa, Hokkaido 071-8142 (Japan)
  2. Japan Biological Information Research Center (JBIRC), Japan Biological Informatics Consortium (JBIC), 2-42 Aomi, Koto-ku, Tokyo 135-0064 (Japan)
  3. Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188 (Japan)
  4. Biological Information Research Center (BIRC), National Institute of Advanced Industrial Science and Technology (AIST), 2-42 Aomi, Koto-ku, Tokyo (Japan)
Publication Date:
OSTI Identifier:
22356262
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 62; Journal Issue: Pt 2; Other Information: PMCID: PMC2150948; PMID: 16511281; PUBLISHER-ID: fw5058; OAI: oai:pubmedcentral.nih.gov:2150948; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ATOMS; CRYSTALLIZATION; CRYSTALS; DIFFUSION; OXYGEN; RESOLUTION; RINGS; SPACE GROUPS; SPECIFICITY; SUBSTRATES

Citation Formats

Sugimoto, Keisuke, Matsufuzi, Kazuki, Ohnuma, Hiroaki, Senda, Miki, Fukuda, Masao, Senda, Toshiya, and Department of Material Chemistry, Asahikawa National College of Technology, 2-2-1-6 Shunko-dai, Asahikawa, Hokkaido 071-8142. Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219. United Kingdom: N. p., 2006. Web. doi:10.1107/S174430910504323X.
Sugimoto, Keisuke, Matsufuzi, Kazuki, Ohnuma, Hiroaki, Senda, Miki, Fukuda, Masao, Senda, Toshiya, & Department of Material Chemistry, Asahikawa National College of Technology, 2-2-1-6 Shunko-dai, Asahikawa, Hokkaido 071-8142. Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219. United Kingdom. https://doi.org/10.1107/S174430910504323X
Sugimoto, Keisuke, Matsufuzi, Kazuki, Ohnuma, Hiroaki, Senda, Miki, Fukuda, Masao, Senda, Toshiya, and Department of Material Chemistry, Asahikawa National College of Technology, 2-2-1-6 Shunko-dai, Asahikawa, Hokkaido 071-8142. 2006. "Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219". United Kingdom. https://doi.org/10.1107/S174430910504323X.
@article{osti_22356262,
title = {Crystallization and preliminary crystallographic analysis of the catechol 2,3-dioxygenase PheB from Bacillus stearothermophilus BR219},
author = {Sugimoto, Keisuke and Matsufuzi, Kazuki and Ohnuma, Hiroaki and Senda, Miki and Fukuda, Masao and Senda, Toshiya and Department of Material Chemistry, Asahikawa National College of Technology, 2-2-1-6 Shunko-dai, Asahikawa, Hokkaido 071-8142},
abstractNote = {PheB, an extradiol-cleaving catecholic dioxygenase, was crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as a precipitant. The crystal belongs to the orthorhombic system, space group P2{sub 1}2{sub 1}2{sub 1}, and diffracts to 2.3 Å resolution. 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{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 65.5, b = 119.2, c = 158.7 Å. The crystal diffracted to 2.3 Å resolution.},
doi = {10.1107/S174430910504323X},
url = {https://www.osti.gov/biblio/22356262}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 2,
volume = 62,
place = {United Kingdom},
year = {Wed Feb 01 00:00:00 EST 2006},
month = {Wed Feb 01 00:00:00 EST 2006}
}