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Crystal structure of linoleate 13R-manganese lipoxygenase in complex with an adhesion protein.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences. (Oliw)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmaceutical Biosciences.
Swedish Univ Agr Sci, Dept Chem & Biotechnol, SE-75007 Uppsala, Sweden.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (Andersson)
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2016 (English)In: Journal of Lipid Research, ISSN 0022-2275, E-ISSN 1539-7262, Vol. 57, no 8, 1574-1588 p.Article in journal (Refereed) Published
Abstract [en]

The crystal structure of 13R-manganese lipoxygenase (MnLOX) of Gaeumannomyces graminis (Gg) in complex with zonadhesin of Pichia pastoris was solved by molecular replacement. Zonadhesin contains β-strands in two subdomains. A comparison of Gg-MnLOX with the 9S-MnLOX of Magnaporthe oryzae (Mo) shows that the protein fold and the geometry of the metal ligands are conserved. The U-shaped active sites differ mainly due to hydrophobic residues of the substrate channel. The volumes and two hydrophobic side pockets near the catalytic base may sanction oxygenation at C-13 and C-9, respectively. Gly-332 of Gg-MnLOX is positioned in the substrate channel between the entrance and the metal center. Replacements with larger residues could restrict oxygen and substrate to reach the active site. C18 fatty acids are likely positioned with C-11 between Mn(2+)OH2 and Leu-336 for hydrogen abstraction and with one side of the 12Z double bond shielded by Phe-337 to prevent antarafacial oxygenation at C-13 and C-11. Phe-347 is positioned at the end of the substrate channel and replacement with smaller residues can position C18 fatty acids for oxygenation at C-9. Gg-MnLOX does not catalyze the sequential lipoxygenation of n-3 fatty acids in contrast to Mo-MnLOX, which illustrates the different configurations of their substrate channels.

Place, publisher, year, edition, pages
2016. Vol. 57, no 8, 1574-1588 p.
National Category
Agricultural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-300962DOI: 10.1194/jlr.M069617ISI: 000380752300023PubMedID: 27313058OAI: oai:DiVA.org:uu-300962DiVA: diva2:953028
Funder
Swedish Research Council, K2013-67X-06523-31-3Knut and Alice Wallenberg Foundation, KAW 2004.0123, KAW 2012.0110
Note

De två första författarna delar förstaförfattarskapet.

Available from: 2016-08-16 Created: 2016-08-16 Last updated: 2016-09-14Bibliographically approved

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Chen, YangEngström, ÅkeOliw, Ernst H
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Department of Pharmaceutical BiosciencesDepartment of Medical Biochemistry and Microbiology
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