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3-DIMENSIONAL STRUCTURE OF CHOLERA-TOXIN PENETRATING A LIPID-MEMBRANE SCIENCE RIBI, H. O., Ludwig, D. S., Mercer, K. L., SCHOOLNIK, G. K., Kornberg, R. D. 1988; 239 (4845): 1272-1276

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.

View details for Web of Science ID A1988M425400021

View details for PubMedID 3344432