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What is Beta-Barrel Outer Membrane Proteins

Handbook of Research on Systems Biology Applications in Medicine
They constitute one of the two major structural classes of transmembrane proteins (the other being the alpha-helical membrane proteins). They have their membrane-spanning segments entirely composed of short amphipathic beta-strands that twist and coil in order to form a barrel (beta-barrel). They have been found up to now only in the outer membranes of Gram-negative Bacteria and presumably (based on low resolution experimental data) on the outer surfaces of mitochondria and chloroplasts. They perform a series of very important biological functions such as membrane transport, receptor activity, and enzyme function or have a structural role. The smallest known transmembrane beta-barrels are composed of 8 beta-strands, whereas the largest are composed of 24 beta-strands even though it is possible that barrels with a larger number exist.
Published in Chapter:
Bacterial ß-Barrel Outer Membrane Proteins: A Common Structural Theme Implicated in a Wide Variety of Functional Roles
Pantelis G. Bagos (University of Central Greece, and University of Athens, Greece) and Stavros J. Hamodrakas (University of Athens, Greece)
Copyright: © 2009 |Pages: 26
DOI: 10.4018/978-1-60566-076-9.ch010
Abstract
ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts. During the last few years, remarkable advances have been made towards an understanding of their functional and structural features. It is now wellknown that ß-barrels are performing a large variety of biologically important functions for the bacterial cell. Such functions include acting as specific or non-specific channels, receptors for various compounds, enzymes, translocation channels, structural proteins, and adhesion proteins. All these functional roles are of great importance for the survival of the bacterial cell under various environmental conditions or for the pathogenic properties expressed by these organisms. This chapter reviews the currently available literature regarding the structure and function of bacterial outer membrane proteins. We emphasize the functional diversity expressed by a common structural motif such as the ß-barrel, and we provide evidence from the current literature for dozens of newly discovered families of transmembrane ß-barrels.
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