Structure-function relationships of the outer membrane translocon Wza investigated by cryo-electron microscopy and mutagenesis.

ABSTRACT: The outer membrane protein Wza, from Escherichia coli K30, forms an octameric complex that is essential for capsular polysaccharide export. Homologs of Wza are widespread in gram-negative bacterial pathogens where capsules are critical virulence determinants. Wza is unusual in that it spans the outer membrane using a barrel composed of amphipathic alpha-helices, rather than being a beta-barrel like almost all other outer membrane channels. The transmembrane helical barrel of Wza also forms the external opening to a hydrophilic translocation pathway that spans the periplasm. Here, we have probed the structure and function of the Wza complex using both cryo-electron microscopy and mutagenesis. The helical barrel structure is stable in detergent micelles under mildly acidic conditions but is

SUBMITTER: Ford RC 

PROVIDER: S-EPMC3498625 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature