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Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa

AuthorsGarreta, Albert ; García-Fernández, Queralt; Fita, Ignacio ; Carpena, Xavi
KeywordsMembrane interaction
Enzyme mechanisms
Host-pathogen interactions
Lipid peroxidation
Protein-phospholipid complexes
Issue DateDec-2013
PublisherFederation of American Societies for Experimental Biology
CitationFASEB Journal 27(12): 4811-4821 (2013)
AbstractLipoxygenases (LOXs), which are essential in eukaryotes, have no confirmed function in prokaryotes that are devoid of polyunsaturated fatty acids. The structure of a secretable LOX from Pseudomonas aeruginosa (Pa-LOX), the first available from a prokaryote, presents significant differences with respect to eukaryotic LOXs, including a cluster of helices acting as a lid to the active center. The mobility of the lid and the structural variability of the N-terminal region of Pa-LOX was confirmed by comparing 2 crystal forms. The binding pocket contains a phosphatidylethanolamine phospholipid with branches of 18 (sn-1) and 14/16 (sn-2) carbon atoms in length. Carbon atoms from the sn-1 chain approach the catalytic iron in a manner that sheds light on how the enzymatic reaction might proceed. The findings in these studies suggest that Pa-LOX has the capacity to extract and modify unsaturated phospholipids from eukaryotic membranes, allowing this LOX to play a role in the interaction of P. Aeruginosa with host cells.Garreta, A., Val-Moraes, S. P., García-Fernández, Q., Montserrat Busquets, C. J., Oliver, A., Ortiz, A., Gaffney, B. J., Fita, I., Manresa, A., Carpena, X. Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa. © FASEB.
DescriptionAlbert Garreta et al.
Publisher version (URL)http://dx.doi.org/10.1096/fj.13-235952
Identifiersdoi: 10.1096/fj.13-235952
issn: 1530-6860
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