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Title: Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β-hydrolase family

Abstract

Preliminary crystallographic data for 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from P. putida 33/1 are reported. 1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 catalyses the oxygenolysis of 1H-3-hydroxy-4-oxoquinoline to form N-formylanthranilic acid and carbon monoxide without the aid of cofactors. Both N-terminally His{sub 6}-tagged and native QDO were overexpressed in Escherichia coli and purified by conventional chromatographic procedures. Untagged QDO, but not His{sub 6}-tagged QDO, was crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6{sub 1}22. Selenomethionine-containing native QDO was prepared and crystallized under identical conditions. The unit-cell parameters were a = b = 90.1, c = 168.6 Å, α = β = 90, γ = 120°. Using synchrotron radiation, these crystals diffract to 2.5 Å. The expression, purification and crystallization of QDO are reported here.

Authors:
 [1];  [2];  [1]
+ Show Author Affiliations
  1. Research School of Chemistry, Australian National University, Acton, ACT 0200 (Australia)
  2. Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, D-48149 Münster (Germany)
Publication Date:
OSTI Identifier:
22360328
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2335004; PMID: 17565175; PUBLISHER-ID: gj5016; OAI: oai:pubmedcentral.nih.gov:2335004; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CARBON MONOXIDE; CRYSTALLIZATION; CRYSTALS; DIFFRACTION; DIFFUSION; ESCHERICHIA COLI; OXYGEN; SPACE GROUPS; SYNCHROTRON RADIATION

Citation Formats

Qi, Ruhu, Fetzner, Susanne, and Oakley, Aaron J., E-mail: oakley@rsc.anu.edu.au. Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β-hydrolase family. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107013760.
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Qi, Ruhu, Fetzner, Susanne, & Oakley, Aaron J., E-mail: oakley@rsc.anu.edu.au. Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β-hydrolase family. United Kingdom. doi:10.1107/S1744309107013760.
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Qi, Ruhu, Fetzner, Susanne, and Oakley, Aaron J., E-mail: oakley@rsc.anu.edu.au. Tue . "Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β-hydrolase family". United Kingdom. doi:10.1107/S1744309107013760.
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@article{osti_22360328,
title = {Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β-hydrolase family},
author = {Qi, Ruhu and Fetzner, Susanne and Oakley, Aaron J., E-mail: oakley@rsc.anu.edu.au},
abstractNote = {Preliminary crystallographic data for 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from P. putida 33/1 are reported. 1H-3-Hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 catalyses the oxygenolysis of 1H-3-hydroxy-4-oxoquinoline to form N-formylanthranilic acid and carbon monoxide without the aid of cofactors. Both N-terminally His{sub 6}-tagged and native QDO were overexpressed in Escherichia coli and purified by conventional chromatographic procedures. Untagged QDO, but not His{sub 6}-tagged QDO, was crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6{sub 1}22. Selenomethionine-containing native QDO was prepared and crystallized under identical conditions. The unit-cell parameters were a = b = 90.1, c = 168.6 Å, α = β = 90, γ = 120°. Using synchrotron radiation, these crystals diffract to 2.5 Å. The expression, purification and crystallization of QDO are reported here.},
doi = {10.1107/S1744309107013760},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}
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Journal Article:
DOI:  10.1107/S1744309107013760
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