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4J3O

Crystal structure of the FimD usher traversed by the pilus tip complex assembly composed of FimC:FimF:FimG:FimH

Summary for 4J3O
Entry DOI10.2210/pdb4j3o/pdb
DescriptorProtein FimG, Protein FimH, Chaperone protein FimC, ... (5 entities in total)
Functional Keywordsbeta barrel, immunglobuline-like fold, type 1 pilus assembly, pilus subunit translocation, adhesion, d-mannose-binding, bacterial outer membrane, cell adhesion-chaperone-membrane protein complex, cell adhesion/chaperone/membrane protein
Biological sourceEscherichia coli
More
Cellular locationFimbrium: P08190 P08191 P08189
Periplasm: P31697
Cell outer membrane; Multi-pass membrane protein (By similarity): P30130
Total number of polymer chains5
Total formula weight176345.78
Authors
Geibel, S.,Waksman, G. (deposition date: 2013-02-06, release date: 2013-04-10, Last modification date: 2024-11-27)
Primary citationGeibel, S.,Procko, E.,Hultgren, S.J.,Baker, D.,Waksman, G.
Structural and energetic basis of folded-protein transport by the FimD usher.
Nature, 496:243-246, 2013
Cited by
PubMed Abstract: Type 1 pili, produced by uropathogenic Escherichia coli, are multisubunit fibres crucial in recognition of and adhesion to host tissues. During pilus biogenesis, subunits are recruited to an outer membrane assembly platform, the FimD usher, which catalyses their polymerization and mediates pilus secretion. The recent determination of the crystal structure of an initiation complex provided insight into the initiation step of pilus biogenesis resulting in pore activation, but very little is known about the elongation steps that follow. Here, to address this question, we determine the structure of an elongation complex in which the tip complex assembly composed of FimC, FimF, FimG and FimH passes through FimD. This structure demonstrates the conformational changes required to prevent backsliding of the nascent pilus through the FimD pore and also reveals unexpected properties of the usher pore. We show that the circular binding interface between the pore lumen and the folded substrate participates in transport by defining a low-energy pathway along which the nascent pilus polymer is guided during secretion.
PubMed: 23579681
DOI: 10.1038/nature12007
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.8 Å)
Structure validation

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數據於2025-06-11公開中

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