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Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences. Swedish Univ Agr Sci, Dept Chem & Biotechnol, Box 7015, SE-75007 Uppsala, Sweden.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
2016 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 291, no 15, 8130-8139 p., 26783260Article in journal (Refereed) Published
Abstract [en]

Lipoxygenases (LOX) are non-heme metal enzymes, which oxidize polyunsaturated fatty acids to hydroperoxides. All LOX belong to the same gene family, and they are widely distributed. LOX of animals, plants and prokaryotes contain Fe as the catalytic metal, whereas fungi express LOX with Fe or with Mn. Little is known about metal selection by LOX and the adjustment of the redox potentials of their protein-bound catalytic metals. Thirteen 3D structures of animal, plant, and prokaryotic FeLOX are available but none of MnLOX. The MnLOX of the most important plant pathogen, the rice blast fungus Magnaporthe oryzae (Mo), was expressed in Pichia pastoris. Mo-MnLOX was deglycosylated, purified to homogeneity, and subjected to crystal screening and X-ray diffraction. The structure was solved by sulfur and manganese single-wavelength anomalous dispersion to a resolution of 2.0 Å. The Mn coordinating sphere is similar to Fe ligands of coral 8R-LOX and soybean LOX-1, but not overlapping. The Asn473 is positioned on a short loop (AsnGlnGlyGluPro) instead of an α-helix and forms hydrogen bonds with Gln281. Comparison with Fe-LOX suggest that Phe332 and Phe525 might contribute to the unique suprafacial hydrogen abstraction and oxygenation mechanism of Mo-MnLOX by controlling oxygen access to the pentadiene radical. Modeling suggests that Arg525 is positioned close to Arg182 of 8R-LOX, and both residues likely tether the carboxylate group of the substrate. An oxygen channel could not be identified. We conclude that Mo-MnLOX illustrates a partly unique variation of the structural theme of FeLOX.

Place, publisher, year, edition, pages
2016. Vol. 291, no 15, 8130-8139 p., 26783260
Keyword [en]
crystal structure; enzyme mechanism; fatty acid oxidation; lipoxygenase pathway; metalloenzyme
National Category
Biochemistry and Molecular Biology Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-278176DOI: 10.1074/jbc.M115.707380ISI: 000374056700030PubMedID: 26783260OAI: oai:DiVA.org:uu-278176DiVA: diva2:906198
Funder
Knut and Alice Wallenberg Foundation, KAW2004.0123Swedish Research Council, K2013-67X-06523-31-3
Available from: 2016-02-24 Created: 2016-02-24 Last updated: 2017-11-30Bibliographically approved

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Oliw, Ernst H.Chen, Yang

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