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  • Title: Two-dimensional crystals of cholera toxin B-subunit-receptor complexes: projected structure at 17-A resolution.
    Author: Ludwig DS, Ribi HO, Schoolnik GK, Kornberg RD.
    Journal: Proc Natl Acad Sci U S A; 1986 Nov; 83(22):8585-8. PubMed ID: 3464971.
    Abstract:
    The B subunit of cholera toxin forms two-dimensional crystals when bound to its membrane receptor, ganglioside GM1, in phospholipid layers. A rectangular crystal lattice gives diffraction extending to 15-A resolution in negative stain, and image-processing of electron micrographs reveals a ring of five protein densities. The diameter of the central hole and the outer diameter of the ring are about 20 and 60 A, respectively. These data are consistent with a pentameric, doughnut-shaped structure of the B subunit that lies flat on a membrane surface. A hexagonal crystal lattice is obtained as well, and results of image processing and chemical crosslinking allow two interpretations: the B subunit may exist in both pentameric and hexameric forms or, more likely, the hexagonal lattice may represent a disordered or liquid crystalline form, in which a pentamer undergoes rotational averaging about its 5-fold axis.
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