4g32

Publication Abstract from PubMed

Lipoxygenases (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., Garcia-Fernandez, 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.

Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa.,Garreta A, Val-Moraes SP, Garcia-Fernandez Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa A, Carpena X FASEB J. 2013 Aug 30. PMID:23985801^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.