JSON
Jiang W, Ubhayasekera W, Pearson MM, Knight SD
Acta Crystallogr D Struct Biol 74 (Pt 11) 1053-1062 [2018-11-01; online 2018-10-29]
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.
Protein Science Facility (PSF) [Service]
PubMed 30387764
DOI 10.1107/S2059798318012391
Crossref 10.1107/S2059798318012391
pii: S2059798318012391