Outer membrane translocons: structural insights into channel formation.
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.
Faculty of Life Sciences, The University of Manchester, Oxford Road, Manchester, UK.
Vijaykumar
V
Karuppiah
Jamie-Lee
JL
Berry
Jeremy P
JP
Derrick
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D001693:Biological Transport, Active; D006090:Gram-Negative Bacteria / Q000166:cytology / Q000378:metabolism*; D017433:Protein Structure, Secondary
D001425:Bacterial Outer Membrane Proteins