Microbiology news and views
J. Mol. Micro. Biotechnol. 4: 1-10
Structure and Function of Pore-Forming ß-Barrels from Bacteria
Anne H. Delcour
Crystallographic studies of the past ten years have revealed that many outer membrane proteins and bacterial toxins are constructed on the ß-barrel motif. Two structural classes can be identified. The first class, represented by the porins, includes monomeric or multimeric proteins where each ß-barrel is formed from a single polypeptide. The second class features proteins where the ß-barrel is itself a multimeric assembly, to which each subunit contributes a few ß-strands. In addition to structural investigations, much work has also been devoted to the functional aspects of these proteins, and to the relationships between structure and function. Here we present a review of the structural and the functional properties of some of the best-studied examples of these various classes of proteins, namely the generaldiffusion, specific and ligand-gated porins, multidrug efflux proteins and the staphylococcal toxin a-hemolysin.
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