Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form

J Biol Chem. 2006 Aug 11;281(32):23042-9. doi: 10.1074/jbc.M602421200. Epub 2006 Jun 5.

Abstract

Hemolysin E (HlyE, ClyA, SheA) is a pore-forming protein toxin isolated from Escherichia coli. The three-dimensional structure of its water-soluble form is known, but that of the membrane-bound HlyE complex is not. We have used electron microscopy and image processing to show that the pores are predominantly octameric. Three-dimensional reconstructions of HlyE pores assembled in lipid/detergent micelles suggest a degree of conformational variability in the octameric complexes. The reconstructed pores were significantly longer than the maximum dimension of the water-soluble molecule, indicating that conformational changes occur on pore formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Brain / metabolism
  • Cell Membrane / metabolism*
  • Detergents / pharmacology
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Hemolysin Proteins
  • Hydrolysis
  • Imaging, Three-Dimensional
  • Lipids / chemistry
  • Micelles
  • Microscopy, Electron, Transmission
  • Models, Molecular
  • Protein Conformation
  • Water / chemistry

Substances

  • Bacterial Proteins
  • Detergents
  • Escherichia coli Proteins
  • Hemolysin Proteins
  • Lipids
  • Micelles
  • hlyE protein, E coli
  • Water