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

Journal Article


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Abstract


  • 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 His6-tagged and native QDO were overexpressed in Escherichia coli and purified by conventional chromatographic procedures. Untagged QDO, but not His6-tagged QDO, was crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6(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 A, alpha = beta = 90, gamma = 120 degrees. Using synchrotron radiation, these crystals diffract to 2.5 A. The expression, purification and crystallization of QDO are reported here.

Authors


  •   Qi, Ruhu (external author)
  •   Fetzner, Susanne (external author)
  •   Oakley, Aaron J.

Publication Date


  • 2007

Citation


  • Qi, R., Fetzner, S. & Oakley, A. J. (2007). Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family. Acta CrystallographicaSection F: Structural Biology and Crystallization Communications Online, 63 (5), 378-381.

Scopus Eid


  • 2-s2.0-34248229616

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1937&context=scipapers

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/898

Has Global Citation Frequency


Number Of Pages


  • 3

Start Page


  • 378

End Page


  • 381

Volume


  • 63

Issue


  • 5

Abstract


  • 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 His6-tagged and native QDO were overexpressed in Escherichia coli and purified by conventional chromatographic procedures. Untagged QDO, but not His6-tagged QDO, was crystallized by the vapour-diffusion method, giving hexagonal bipyramid crystals belonging to space group P6(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 A, alpha = beta = 90, gamma = 120 degrees. Using synchrotron radiation, these crystals diffract to 2.5 A. The expression, purification and crystallization of QDO are reported here.

Authors


  •   Qi, Ruhu (external author)
  •   Fetzner, Susanne (external author)
  •   Oakley, Aaron J.

Publication Date


  • 2007

Citation


  • Qi, R., Fetzner, S. & Oakley, A. J. (2007). Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the alpha/beta-hydrolase family. Acta CrystallographicaSection F: Structural Biology and Crystallization Communications Online, 63 (5), 378-381.

Scopus Eid


  • 2-s2.0-34248229616

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=1937&context=scipapers

Ro Metadata Url


  • http://ro.uow.edu.au/scipapers/898

Has Global Citation Frequency


Number Of Pages


  • 3

Start Page


  • 378

End Page


  • 381

Volume


  • 63

Issue


  • 5