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

DOI: 10.1107/S2059798318012391 DOI Help

Authors: Wangshu Jiang (Uppsala University) , Wimal Ubhayasekera (Uppsala University) , Melanie M. Pearson (University of Michigan Medical School) , Stefan D. Knight (Uppsala University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 74 , PAGES 1053 - 1062

State: Published (Approved)
Published: November 2018

Abstract: 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.

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

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography

Other Facilities: ESRF

Added On: 08/11/2018 12:10

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Infectious Diseases Pathogens Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)