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J Biol Chem. 2006 Aug 11;281(32):23042-9. Epub 2006 Jun 5.

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

Author information

1
Department of Molecular Biology and Biotechnology, Krebs Institute for Biomolecular Research, The University of Sheffield, Sheffield S10 2TN, United Kingdom.

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.

PMID:
16754675
DOI:
10.1074/jbc.M602421200
[Indexed for MEDLINE]
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