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Science 11 March 1988:
Vol. 239. no. 4845, pp. 1272 - 1276
DOI: 10.1126/science.3344432
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Articles

Science, Vol 239, Issue 4845, 1272-1276
Copyright © 1988 by American Association for the Advancement of Science

articles

Three-dimensional structure of cholera toxin penetrating a lipid membrane

HO Ribi, DS Ludwig, KL Mercer, GK Schoolnik, and RD Kornberg

Department of Cell Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305.

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.


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