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7LHI

Cryo-EM structure of E. coli P pilus tip assembly intermediate PapC-PapD-PapK-PapF-PapG

Summary for 7LHI
Entry DOI10.2210/pdb7lhi/pdb
EMDB information23339 23340 23341
DescriptorP fimbrial usher protein PapC, P fimbria tip G-adhesin PapG-II, Fimbrial protein, ... (5 entities in total)
Functional Keywordscryo-em, uropathogenic escherichia coli, chaperone-usher, p pilus, chaperone
Biological sourceEscherichia coli
More
Total number of polymer chains5
Total formula weight187659.45
Authors
Du, M.,Yuan, Z.,Werneburg, G.,Henderson, N.,Chauhan, H.,Kovach, A.,Zhao, G.,Johl, J.,Li, H.,Thanassi, D. (deposition date: 2021-01-23, release date: 2021-08-11, Last modification date: 2024-05-29)
Primary citationDu, M.,Yuan, Z.,Werneburg, G.T.,Henderson, N.S.,Chauhan, H.,Kovach, A.,Zhao, G.,Johl, J.,Li, H.,Thanassi, D.G.
Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis.
Nat Commun, 12:5207-5207, 2021
Cited by
PubMed Abstract: Uropathogenic Escherichia coli assemble surface structures termed pili or fimbriae to initiate infection of the urinary tract. P pili facilitate bacterial colonization of the kidney and pyelonephritis. P pili are assembled through the conserved chaperone-usher pathway. Much of the structural and functional understanding of the chaperone-usher pathway has been gained through investigations of type 1 pili, which promote binding to the bladder and cystitis. In contrast, the structural basis for P pilus biogenesis at the usher has remained elusive. This is in part due to the flexible and variable-length P pilus tip fiber, creating structural heterogeneity, and difficulties isolating stable P pilus assembly intermediates. Here, we circumvent these hindrances and determine cryo-electron microscopy structures of the activated PapC usher in the process of secreting two- and three-subunit P pilus assembly intermediates, revealing processive steps in P pilus biogenesis and capturing new conformational dynamics of the usher assembly machine.
PubMed: 34471127
DOI: 10.1038/s41467-021-25522-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.6 Å)
Structure validation

226707

数据于2024-10-30公开中

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