Abstract
Crystallographic and associated biochemical and structural studies are in progress on the fiber-forming pilin proteins of the gonococcal pilus. Preparative scale purification procedures have been developed for the gonococcal pilin protein, which appear generally applicable to bacterial pilins. For three gonococcal pilin protein strains, we have obtained both reassembled pilus fibers and three-dimensional crystals. One needle-shaped crystal form of gonococcal C30 pilin diffracts beyond 3 Å resolution using synchrotron x-ray radiation. A diffraction data set to 3.5 Å resolution has been collected on these needle-shaped crystals (lattice spacings a=125.4(3) b=120.4(3), c=26.61(4) Å) in which the packing arrangement of the pilin subunits appears to resemble that seen in the pilus fibers using electron microscopy. X-ray diffraction data confirm our proposed model for the overall polypeptide fold of a pilin subunit, which is an antiparallel 4-α helix bundle similar to tobacco mosaic virus coat protein and myohemerythrin.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Bloomer, A. C., J. N. Champness, G. Bricogne, R. Staden & A. Klug (1978) Protein disk of tobacco mosaic virus at 2.8 Å esolation showing the interactions within and between subunits. Nature 276: 362–368
Brinton, C. C., J. Bryan, J. Dillon, N. Guerina, L. J. Jacobson, A. Labik, S. Lee, A. Levine, S. Lim, J. McMichael, S. Polen, K. Rogers, A. C. To & S. C. To (1978) Uses of pili in gonorrhea control. Role of bacterial pili in disease, purification and properties of gonococcal pili, and progress in the development of a gonococcal pilus vaccine for gonorrhea. In: G. F. Brooks & E. C. Gotschlich (Eds), Immunobiology of N. gonorrhoeae (pp. 155–178). American Society for Microbiology, Washington, D.C.
Deal, C. D., J. A. Tainer, M. So & E. D. Getzoff (1985) Identification of a common structural class for Neisseria gonorrheae and other bacterial pilins. In: G. K. Schoolnik (Ed) The Pathogenic Neisseriae (pp. 302–308). American Society for Microbiology, Washington, D.C.
Getzoff, E. D., H. M. Geysen, S. J. Rodda, H. Alexander, J. A. Tainer & R. A. Lerner (1987) Mechanisms of antibody binding to a protein. Science 235: 1191–1196
Hagblom, P., E. Segal, E. Billyard & M. So (1985) Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae. Nature 315: 156–158
McPherson, A. (1976) The growth and preliminary investigation of protein and nucleic acid crystals for X-ray diffraction analysis. Methods of Biochem. Analysis 23: 249–345
Parge, H. E., D. E. McRee, C. D. Deal, M. So, E. D. Getzoff & J. A. Tainer (1987) Crystallization and structural model for Neisseria gonorrheae pilin. Nature (in preparation)
Rothbard, J. B., R. Fernandez & G. K. Schoolnik (1984) Strain-Specific and common epitopes of gonococcal pili. J. of Exp. Med. 160: 208–221
Schoolnik, G. K., R. Fernandez, J. Y. Tai, J. Rothbard & E. C. Gotschlich (1984) Gonococcal pili. Primary structure and receptor binding domain. J. of Exp. Med. 159: 1351–1370
Tainer, J. A., E. D. Getzoff, H. Alexander, R. A. Houghten, A. J. Olson, R. A. Lerner & W. A. Hendrickson (1984) The reactivity of anti-peptide antibodies is a function of the atomic mobility of sites in a protein. Nature. 312: 127
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Parge, H.E., McRee, D.E., Capozza, M.A. et al. Three dimensional structure of bacterial pili. Antonie van Leeuwenhoek 53, 447–453 (1987). https://doi.org/10.1007/BF00415501
Issue Date:
DOI: https://doi.org/10.1007/BF00415501