Staphylococcus aureus alpha-toxin: characterization of protein/lipid interactions, 2D crystallization on lipid monolayers, and 3D structure

Journal of Structural Biology
M J EllisM Thelestam

Abstract

Staphylococcus aureus alpha-toxin was characterized with respect to surface activity and its interaction with lipid monolayers. The protein alone had a detergent-like behavior at the air/water interface. Its affinity was higher for negatively charged than for neutral phospholipids. The interaction was pH dependent, showing a maximum increase at pH 7.0. Only a small part of the protein oligomer appeared to be inserted into the monolayers. Crystalline sheets of alpha-toxin were formed using negatively charged phospholipids. Electron microscopy of such areas, at different tilt angles, allowed reconstruction of a three-dimensional model following image processing. The sheets analyzed consisted of two protein layers arranged on a tetragonal lattice. Under the conditions used to grow the crystals the toxin formed 90-A-wide cylinders with a height of 70 A. One of the imposed fourfold axes running perpendicular to the plane of the crystalline layer is positioned at a protein-deficient region which forms a 25-A-wide pore through the oligomer.

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Citations

Mar 27, 2010·The Journal of Membrane Biology·Beatrix Vécsey-SemjénRoland Möllby
Feb 13, 2001·Micron : the International Research and Review Journal for Microscopy·M J Ellis, H Hebert
Oct 31, 2002·Journal of Structural Biology·Xavier HagnerelleDaniel Lévy
Oct 21, 1999·Methods : a Companion to Methods in Enzymology·H O Spivey, J Ovádi

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