Abstract
Gram-negative bacteria need to maintain the integrity of their outer membrane while also regulating the secretion of toxins and other macromolecules. A variety of dedicated outer membrane proteins (OMPs) facilitate this process. Recent structural work has shown that some of these proteins adopt classical β-barrel transmembrane structures and rely on structural changes within the barrel lumen to allow passage of substrate proteins. Other secretion systems have OMP components which use transmembrane α-helices and appear to function in a different way. Here we review a selection of recent structural studies which have major ramifications for our understanding of the passage of macromolecules across the outer membrane. © 2010 Elsevier Ltd.
Original language | English |
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Pages (from-to) | 40-48 |
Number of pages | 8 |
Journal | Trends in Microbiology |
Volume | 19 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jan 2011 |