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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

NCBI PubMed ID: 16091033
Journal NLM ID: 8712028
Publisher: Blackwell Publishing
Correspondence: russell.bishop

utoronto.ca
Institutions: Departments of Laboratory Medicine and Pathobiology, and Biochemistry, University of Toronto, Toronto, Ontario, M5S 1A8, Canada

Palmitoylated lipid A can both protect pathogenic bacteria from host immune defences and attenuate the activation of those same defences through the TLR4 signal transduction pathway. A palmitate chain from a phospholipid is incorporated into lipid A by an outer membrane enzyme PagP, which is an 8-stranded antiparallel beta-barrel preceded by an amino-terminal amphipathic alpha-helix. The PagP barrel axis is tilted by 25 degrees with respect to the membrane normal. An interior hydrophobic pocket in the outer leaflet-exposed half of the molecule functions as a hydrocarbon ruler that allows the enzyme to distinguish palmitate from other acyl chains found in phospholipids. Internalization of a phospholipid palmitoyl group within the barrel appears to occur by lateral diffusion from the outer leaflet through non-hydrogen-bonded regions between beta-strands. The MsbA-dependent trafficking of lipids from the inner membrane to the outer membrane outer leaflet is necessary for lipid A palmitoylation in vivo. The mechanisms by which bacteria regulate pagP gene expression strikingly reflect the corresponding pathogenic lifestyle of the bacterium. Variations on PagP structure and function can be illustrated with the known homologues from Gram-negative bacteria, which include pathogens of humans and other mammals in addition to pathogens of insects and plants. The PagP enzyme is potentially a target for the development of anti-infective agents, a probe of outer membrane lipid asymmetry, and a tool for the synthesis of lipid A-based vaccine adjuvants and endotoxin antagonists

structure, Pathogenesis, lipid A, plant, outer membrane, phospholipid, signal transduction, palmitoyltransferase PagP

Structure type: oligomer
Location inside paper: p.901, fig.1, Kdo2-lipid A (Re endotoxin)
Trivial name: inner core, Kdo2-lipid A
Compound class: core oligosaccharide, LOS, lipid A
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141807,IEDB_150908,IEDB_151531,IEDB_176772,IEDB_534864

Comments, role: MicroReview

Related record ID(s): 31273
NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases

There is only one chemically distinct structure:

CCCCCCCCCCCCCC(=O)O[C@H](CCCCCCCCCCC)CC(=O)O[C@H]1[C@H](OP(=O)(O)O)[C@@H](CO[C@]2(C(=O)O)C[C@@H](O[C@]3(C(=O)O)C[C@@H](O)[C@@H](O)[C@@H]([C@H](O)CO)O3)[C@@H](O)[C@@H]([C@H](O)CO)O2)O[C@@H](OC[C@H]2O[C@H](OP(=O)(O)O)[C@H](NC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H](OC(=O)C[C@H](O)CCCCCCCCCCC)[C@@H]2O)[C@@H]1NC(=O)C[C@@H](CCCCCCCCCCC)OC(=O)CCCCCCCCCCC

SVG MW SMILES 3D mol Ionize