6H1X
Receptor-binding domain of Proteus mirabilis Uroepithelial Cell Adhesin UcaD21-211
Summary for 6H1X
| Entry DOI | 10.2210/pdb6h1x/pdb |
| Descriptor | Putative fimbrial adhesin, COBALT (II) ION (3 entities in total) |
| Functional Keywords | fimbriae, adhesin, proteus mirabilis, urinary tract infection, cell adhesion |
| Biological source | Proteus mirabilis |
| Total number of polymer chains | 1 |
| Total formula weight | 21245.76 |
| Authors | Wangshu, J.,Knight, S.D. (deposition date: 2018-07-12, release date: 2018-11-07, Last modification date: 2024-05-15) |
| Primary citation | Jiang, W.,Ubhayasekera, W.,Pearson, M.M.,Knight, S.D. Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis. Acta Crystallogr D Struct Biol, 74:1053-1062, 2018 Cited by PubMed 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. PubMed: 30387764DOI: 10.1107/S2059798318012391 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
