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

Naturevolume 378pages3238 (1995) | Download Citation

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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

    • Hans E. Parge

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

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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https://doi.org/10.1038/378032a0

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