Structure of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form.
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.
Tzokov
Svetomir B
SB
Department of Molecular Biology and Biotechnology, Krebs Institute for Biomolecular Research, The University of Sheffield, Sheffield S10 2TN, United Kingdom.
Wyborn
Neil R
NR
Stillman
Timothy J
TJ
Jamieson
Stuart
S
Czudnochowski
Nadine
N
Artymiuk
Peter J
PJ
Green
Jeffrey
J
Bullough
Per A
PA
D001426:Bacterial Proteins / Q000737:chemistry; D001921:Brain / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D003902:Detergents / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006460:Hemolysin Proteins; D006868:Hydrolysis; D021621:Imaging, Three-Dimensional; D008055:Lipids / Q000737:chemistry; D008823:Micelles; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D011487:Protein Conformation; D014867:Water / Q000737:chemistry
D001426:Bacterial Proteins; D003902:Detergents; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; D008055:Lipids; D008823:Micelles; C119944:hlyE protein, E coli; D014867:Water