4G32

Crystal Structure of a Phospholipid-Lipoxygenase Complex from Pseudomonas aeruginosa at 1.75A (P21212)

Summary for 4G32

• Entry DOI: 10.2210/pdb4g32/pdb
• Related: 4G33
• Descriptor: 15S-LIPOXYGENASE, FE (II) ION, (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradec-5-enoyloxy)propyl (11Z)-octadec-11-enoate, ... (5 entities in total)
• Functional Keywords: non-heme iron enzyme, protein-phospholipid complex, oxidoreductase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 76994.49

Authors

Carpena, X.,Garreta, A.,Val-Moraes, S.P.,Garcia-Fernandez, Q.,Fita, I. (deposition date: 2012-07-13, release date: 2013-11-06, Last modification date: 2023-09-13)

Primary citation

Garreta, A.,Val-Moraes, S.P.,Garcia-Fernandez, Q.,Busquets, M.,Juan, C.,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 J., 27:4811-4821, 2013

PubMed Abstract: 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.

PubMed: 23985801
DOI: 10.1096/fj.13-235952

Experimental method

X-RAY DIFFRACTION (1.75 Å)