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

doi:10.1107/S1744309107013760

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

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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:

Qi, Ruhu ^[1]; Fetzner, Susanne ^[2]; Oakley, Aaron J., E-mail: oakley@rsc.anu.edu.au ^[1]

Research School of Chemistry, Australian National University, Acton, ACT 0200 (Australia)
Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, D-48149 Münster (Germany)

Publication Date:: Tue May 01 00:00:00 EDT 2007

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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DOI: 10.1107/S1744309107013760

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