Three-Dimensional Structure of Cholera Toxin Penetrating a Lipid Membrane
- 11 March 1988
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 239 (4845), 1272-1276
- https://doi.org/10.1126/science.3344432
Abstract
Two-dimensional crystals of cholera toxin bound to receptors in a lipid membrane give diffraction extending to 15 A resolution. Three-dimensional structure determination reveals a ring of five B subunits on the membrane surface, with one-third of the A subunit occupying the center of the ring. The remaining mass of the A subunit appears to penetrate the hydrophobic interior of the membrane. Cleavage of a disulfide bond in the A subunit, which activates the toxin, causes a major conformational change, with the A subunit mostly exiting from the B ring.This publication has 33 references indexed in Scilit:
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