8ptu
From Proteopedia
2.5 A cryo-EM structure of the in vitro FimD-catalyzed assembly of type 1 pilus rod
Structural highlights
FunctionFIMA1_ECOLI Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. Publication Abstract from PubMedType 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA and is assembled in vivo by the assembly platform FimD. Although type 1 pilus rods can self-assemble from FimA in vitro, this reaction is slower and produces structures with lower kinetic stability against denaturants compared to in vivo-assembled rods. Our study reveals that FimD-catalysed in vitro-assembled type 1 pilus rods attain a similar stability as pilus rods assembled in vivo. Employing structural, biophysical and biochemical analyses, we show that in vitro assembly reactions lacking FimD produce pilus rods with structural defects, reducing their stability against dissociation. Overall, our results indicate that FimD is not only required for the catalysis of pilus assembly, but also to control the assembly of the most stable quaternary structure. The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.,Zyla DS, Wiegand T, Bachmann P, Zdanowicz R, Giese C, Meier BH, Waksman G, Hospenthal MK, Glockshuber R Nat Commun. 2024 Apr 8;15(1):3032. doi: 10.1038/s41467-024-47212-9. PMID:38589417[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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