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