5OH0

The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod

Summary for 5OH0

• Entry DOI: 10.2210/pdb5oh0/pdb
• EMDB information: 3809
• Descriptor: Type-1 fimbrial protein, A chain (1 entity in total)
• Functional Keywords: bacterial pilus, chaperone-usher pilus, protein fibril
• Biological source: Escherichia coli J96
• Total number of polymer chains: 6
• Total formula weight: 95011.46

Authors

Hospenthal, M.K.,Costa, T.R.D.,Redzej, A.,Waksman, G. (deposition date: 2017-07-13, release date: 2017-11-22, Last modification date: 2024-11-20)

Primary citation

Hospenthal, M.K.,Zyla, D.,Costa, T.R.D.,Redzej, A.,Giese, C.,Lillington, J.,Glockshuber, R.,Waksman, G.
The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.
Structure, 25:1829-1838.e4, 2017

PubMed Abstract: Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable "spring-like" properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro.

PubMed: 29129382
DOI: 10.1016/j.str.2017.10.004

Experimental method

ELECTRON MICROSCOPY (4.2 Å)