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Members of this family are enzymes catalyzing the removal of the fatty acyl chain from the 3rd position of lipid A, the highly conserved lipid moiety of the lipopolysaccharide (LPS), which is one of the main constituents of the Gram-negative bacterial outer membrane. The first identified member of the family was the outer membrane-localized lipid A 3-O-deacylase, which is encoded by the PagL gene of Salmonella enterica serovar typhimurium. Homologs have been discovered in a variety of Gram-negative bacteria, although the overall sequence similarity is rather low. When expressed in Escherichia coli and upon deacylation by PagL, lipid A underwent another modification, which was the result of the activity of the endogenous palmitoyl-transferase PagP. A conserved histidine-serine couple was identified as the active site suggesting a catalytic mechanism similar to serine hydrolases. The exact biological function of PagL remains unclear, while its high-resolution structure revealed a dimeric structure with ß-barrels comprising 8 transmembrane strands.
A PhoP/PhoQ-induced Lipase (PagL) that catalyzes 3-O-deacylation of lipid A precursors in membranes of Salmonella typhimurium
J Biol Chem. 2001 Mar 23;276(12):9083-92. doi: 10.1074/jbc.M010730200. Epub 2000 Dec 6.
Dissemination of lipid A deacylases (pagL) among gram-negative bacteria: identification of active-site histidine and serine residues
J Biol Chem. 2005 Mar 4;280(9):8248-59. doi: 10.1074/jbc.M414235200. Epub 2004 Dec 20.
Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane
Biochim Biophys Acta. 2008 Sep;1778(9):1881-96. doi: 10.1016/j.bbamem.2007.07.021. Epub 2007 Aug 11.
Crystal structure and catalytic mechanism of the LPS 3-O-deacylase PagL from Pseudomonas aeruginosa
Proc Natl Acad Sci U S A. 2006 May 2;103(18):7071-6. doi: 10.1073/pnas.0509392103. Epub 2006 Apr 21.
|Proteins in this family with 3D-structure|