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Crystallization and preliminary crystallographic analysis of manganese lipoxygenase

Authors :
Ernst H. Oliw
Anneli Wennman
Saeid Karkehabadi
Source :
Acta crystallographica. Section F, Structural biology communications. 70(Pt 4)
Publication Year :
2014

Abstract

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. APichia pastorisexpression 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 α-mannosidase, purified to apparent homogeneity and subjected to crystal screening and X-ray diffraction. The crystals diffracted to 2.6 Å resolution and belonged to space groupC2, with unit-cell parametersa= 226.6,b= 50.6,c= 177.92 Å, β = 91.70°.

Details

ISSN :
2053230X
Volume :
70
Issue :
Pt 4
Database :
OpenAIRE
Journal :
Acta crystallographica. Section F, Structural biology communications
Accession number :
edsair.doi.dedup.....9885cc7de5056deaac42fbbd24d6e7e6