Crystallization and preliminary crystallographic analysis of manganese lipoxygenase
2014 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 70, 522-525 p.Article in journal (Refereed) Published
Lipoxygenases constitute a family of nonhaem metal enzymes with catalytic iron or, occasionally, catalytic manganese. Lipoxygenases oxidize polyunsaturated fatty acids with position specificity and stereospecificity to hydroperoxides, which contribute to inflammation and the development of cancer. Little is known about the structural differences between lipoxygenases with Fe or Mn and the metal-selection mechanism. A Pichia pastoris expression system was used for the production of the manganese lipoxygenase of the take-all fungus of wheat, Gaeumannomyces graminis. The active enzyme was treated with alpha-mannosidase, purified to apparent homogeneity and subjected to crystal screening and X-ray diffraction. The crystals diffracted to 2.6 angstrom resolution and belonged to space group C2, with unit-cell parameters a = 226.6, b = 50.6, c = 177.92 angstrom, beta = 91.70 degrees.
Place, publisher, year, edition, pages
2014. Vol. 70, 522-525 p.
IdentifiersURN: urn:nbn:se:uu:diva-224330DOI: 10.1107/S2053230X14005548ISI: 000333757800027OAI: oai:DiVA.org:uu-224330DiVA: diva2:717094