Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis

Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1053-1062. doi: 10.1107/S2059798318012391. Epub 2018 Oct 29.


The important uropathogen Proteus mirabilis encodes a record number of chaperone/usher-pathway adhesive fimbriae. Such fimbriae, which are used for adhesion to cell surfaces/tissues and for biofilm formation, are typically important virulence factors in bacterial pathogenesis. Here, the structures of the receptor-binding domains of the tip-located two-domain adhesins UcaD (1.5 Å resolution) and AtfE (1.58 Å resolution) from two P. mirabilis fimbriae (UCA/NAF and ATF) are presented. The structures of UcaD and AtfE are both similar to the F17G type of tip-located fimbrial receptor-binding domains, and the structures are very similar despite having only limited sequence similarity. These structures represent an important step towards a molecular-level understanding of P. mirabilis fimbrial adhesins and their roles in the complex pathogenesis of urinary-tract infections.

Keywords: Proteus mirabilis; adhesins; fimbriae; urinary-tract infection.

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / classification
  • Adhesins, Bacterial / metabolism
  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Protein Conformation*
  • Proteus mirabilis / growth & development
  • Proteus mirabilis / metabolism*
  • Sequence Homology


  • Adhesins, Bacterial