Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis. Issue 11 (2nd November 2018)

• Record Type: Journal Article
• Authors: Jiang, Wangshu; Ubhayasekera, Wimal; Pearson, Melanie M.; Knight, Stefan D.
• Is Part Of: Acta crystallographica. Volume 74:Issue 11(2018)
• Page Start: 1053
• Page End: 1062
• Publication Date: 2018-11-02
• Subjects: fimbriae -- adhesins -- urinary‐tract infection -- Proteus mirabilis; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; Molecular biology -- Periodicals; Molecular structure -- Periodicals; Biomolecules -- Structure -- Periodicals; Cytology -- Periodicals; Biomolecules -- Structure; Crystallography; Cytology; Molecular biology; Molecular structure; X-ray crystallography; Periodicals; 548
• DOI: 10.1107/S2059798318012391
• Languages: English
• ISSNs: 2059-7983

Abstract

Abstract : The crystal structures of two fimbrial adhesins from the uropathogen P. mirabilis are reported as a first step towards unveiling their role in pathogenesis. Despite lacking significant sequence homology, the two structures are very similar. 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.