Outer membrane translocons: structural insights into channel formation

Trends Microbiol. 2011 Jan;19(1):40-8. doi: 10.1016/j.tim.2010.10.006. Epub 2010 Dec 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / metabolism*
  • Biological Transport, Active
  • Gram-Negative Bacteria / cytology
  • Gram-Negative Bacteria / metabolism*
  • Protein Structure, Secondary

Substances

  • Bacterial Outer Membrane Proteins