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Structure of the fibre-forming protein pilin at 2.6 Å resolution

Nature volume 378, pages 32–38 (1995)Cite this article

Abstract

The crystallographic structure of Neisseria gonorrhoeae pilin, which assembles into the multi-functional pilus adhesion and virulence factor, reveals an α–β roll fold with a striking 85 Å α-helical spine and an 0-linked disaccharide. Key residues stabilize interactions that allow sequence hypervariability, responsible for pilin's celebrated antigenic variation, within disulphide region β-strands and connections. Pilin surface shape, hydrophobicity and sequence variation constrain pilus assembly to the packing of flat subunit faces against α1 helices. Helical fibre assembly is postulated to form a core of coiled α1 helices banded by β-sheet, leaving carbohydrate and hypervariable sequence regions exposed to solvent.

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Author notes

  1. Hans E. Parge

    Present address: Agouron Pharmaceuticals Inc., Research Laboratories, 3565 General Atomics Court, San Diego, California, 92121-1121, USA

Authors and Affiliations

  1. Department of Molecular Biology, The Scripps Research Institute, La Jolla, California, 92037, USA

    Hans E. Parge, Katrina T. Forest, Michael J. Hickey, Deborah A. Christensen, Elizabeth D. Getzoff & John A. Tainer

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Parge, H., Forest, K., Hickey, M. et al. Structure of the fibre-forming protein pilin at 2.6 Å resolution. Nature 378, 32–38 (1995). https://doi.org/10.1038/378032a0

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