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

Nature. 1995 Nov 2;378(6552):32-8. doi: 10.1038/378032a0.


The crystallographic structure of Neisseria gonorrhoeae pilin, which assembles into the multifunctional pilus adhesion and virulence factor, reveals an alpha-beta roll fold with a striking 85 A alpha-helical spine and an O-linked disaccharide. Key residues stabilize interactions that allow sequence hypervariability, responsible for pilin's celebrated antigenic variation, within disulphide region beta-strands and connections. Pilin surface shape, hydrophobicity and sequence variation constrain pilus assembly to the packing of flat subunit faces against alpha 1 helices. Helical fibre assembly is postulated to form a core of coiled alpha 1 helices banded by beta-sheet, leaving carbohydrate and hypervariable sequence regions exposed to solvent.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Outer Membrane Proteins / chemistry*
  • Carbohydrate Sequence
  • Computer Simulation
  • Crystallography, X-Ray
  • Disaccharides / chemistry
  • Fimbriae Proteins
  • Fimbriae, Bacterial / chemistry*
  • Molecular Sequence Data
  • Neisseria gonorrhoeae / chemistry*
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Surface Properties


  • Bacterial Outer Membrane Proteins
  • Disaccharides
  • Fimbriae Proteins