Gary Schoolnik

Publication Details

  • TWO-DIMENSIONAL CRYSTALS OF CHOLERA-TOXIN B-SUBUNIT RECEPTOR COMPLEXES - PROJECTED STRUCTURE AT 17-A RESOLUTION PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA Ludwig, D. S., RIBI, H. O., SCHOOLNIK, G. K., Kornberg, R. D. 1986; 83 (22): 8585-8588

    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.

    View details for Web of Science ID A1986E906700032

    View details for PubMedID 3464971

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