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What is Outer Membrane

Handbook of Research on Systems Biology Applications in Medicine
The term refers to the external (outside) membranes of Gram-negative bacteria, chloroplasts and mitochondria. The outer membrane of Gram-negative bacteria has a unique and unusual structure. The outer leaflet of the membrane is composed of a complex lipopolysaccharide (LPS) whose lipid portion acts as an endotoxin. Another noticeable difference of the outer membrane (at least in Bacteria) is the fact that proteins that are embedded in it (integral membrane proteins), are having their membrane-spanning segments entirely composed of beta-strands (beta-barrel outer membrane proteins), as opposed to integral membrane proteins in any other membrane which have their membrane spanning segments formed by hydrophobic alpha-helices (alpha-helical membrane proteins).
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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