Koebnik R Locher KP Van Gelder P 2000 The outer membrane protects Gram-negative bacteria against a harsh environment. At the same time, the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction. Unlike membrane proteins from all other sources, integral outer membrane proteins do not consist of transmembrane alpha-helices, but instead fold into antiparallel beta-barrels. Over recent years, the atomic structures of several outer membrane proteins, belonging to six families, have been determined. They include the OmpA membrane domain, the OmpX protein, phospholipase A, general porins (OmpF, PhoE), substrate-specific porins (LamB, ScrY) and the TonB-dependent iron siderophore transporters FhuA and FepA. These crystallographic studies have yielded invaluable insight into and decisively advanced the understanding of the functions of these intriguing proteins. Our review is aimed at discussing their common principles and peculiarities as well as open questions associated with them. application/pdf https://sonar.ch/global/documents/204656 eng info:eu-repo/semantics/altIdentifier/doi/10.1046/j.1365-2958.2000.01983.x info:eu-repo/semantics/altIdentifier/pmid/10931321 info:eu-repo/semantics/openAccess Molecular microbiology. - 2000 Bacterial Outer Membrane Proteins Bacterial Proteins Biological Transport Conserved Sequence Escherichia coli Proteins Gram-Negative Bacteria Hydrolases Membrane Proteins Models, Molecular Phospholipases A Porins Protein Structure, Secondary Signal Transduction Structure and function of bacterial outer membrane proteins: barrels in a nutshell. http://purl.org/coar/resource_type/c_6501