PMID:17880914
| Citation |
Bishop, RE (2008) Structural biology of membrane-intrinsic beta-barrel enzymes: sentinels of the bacterial outer membrane. Biochim. Biophys. Acta 1778:1881-96 |
|---|---|
| Abstract |
The outer membranes of Gram-negative bacteria are replete with integral membrane proteins that exhibit antiparallel beta-barrel structures, but very few of these proteins function as enzymes. In Escherichia coli, only three beta-barrel enzymes are known to exist in the outer membrane; these are the phospholipase OMPLA, the protease OmpT, and the phospholipidColon, two colonslipid A palmitoyltransferase PagP, all of which have been characterized at the structural level. Structural details have also emerged for the outer membrane beta-barrel enzyme PagL, a lipid A 3-O-deacylase from Pseudomonas aeruginosa. Lipid A can be further modified in the outer membrane by two beta-barrel enzymes of unknown structure; namely, the Salmonella enterica 3'-acyloxyacyl hydrolase LpxR, and the Rhizobium leguminosarum oxidase LpxQ, which employs O(2) to convert the proximal glucosamine unit of lipid A into 2-aminogluconate. Structural biology now indicates how beta-barrel enzymes can function as sentinels that remain dormant when the outer membrane permeability barrier is intact. Host immune defenses and antibiotics that perturb this barrier can directly trigger beta-barrel enzymes in the outer membrane. The ensuing adaptive responses occur instantaneously and rapidly outpace other signal transduction mechanisms that similarly function to restore the outer membrane permeability barrier. |
| Links |
PubMed Online version:10.1016/j.bbamem.2007.07.021 |
| Keywords |
Acyltransferases/chemistry; Acyltransferases/physiology; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Bacterial Outer Membrane Proteins/physiology; Bacterial Proteins/chemistry; Bacterial Proteins/physiology; Carboxylic Ester Hydrolases/chemistry; Carboxylic Ester Hydrolases/physiology; Cell Membrane/chemistry; Cell Membrane/metabolism; Cell Membrane/physiology; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/physiology; Gram-Negative Bacteria/chemistry; Gram-Negative Bacteria/enzymology; Gram-Negative Bacteria/metabolism; Gram-Negative Bacteria/ultrastructure; Models, Biological; Models, Molecular; Phospholipases A1/chemistry; Phospholipases A1/physiology; Porins/chemistry; Porins/physiology; Protein Conformation; Protein Structure, Secondary |
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