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TitleHandover mechanism of the growing pilus by the bacterial outer-membrane usher FimD.
Journal, issue, pagesNature, Vol. 562, Issue 7727, Page 444-447, Year 2018
Publish dateOct 3, 2018
AuthorsMinge Du / Zuanning Yuan / Hongjun Yu / Nadine Henderson / Samema Sarowar / Gongpu Zhao / Glenn T Werneburg / David G Thanassi / Huilin Li /
PubMed AbstractPathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors. Type 1 pili are assembled via the conserved chaperone- ...Pathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors. Type 1 pili are assembled via the conserved chaperone-usher pathway. The outer-membrane usher FimD recruits pilus subunits bound by the chaperone FimC via the periplasmic N-terminal domain of the usher. Subunit translocation through the β-barrel channel of the usher occurs at the two C-terminal domains (which we label CTD1 and CTD2) of this protein. How the chaperone-subunit complex bound to the N-terminal domain is handed over to the C-terminal domains, as well as the timing of subunit polymerization into the growing pilus, have previously been unclear. Here we use cryo-electron microscopy to capture a pilus assembly intermediate (FimD-FimC-FimF-FimG-FimH) in a conformation in which FimD is in the process of handing over the chaperone-bound end of the growing pilus to the C-terminal domains. In this structure, FimF has already polymerized with FimG, and the N-terminal domain of FimD swings over to bind CTD2; the N-terminal domain maintains contact with FimC-FimF, while at the same time permitting access to the C-terminal domains. FimD has an intrinsically disordered N-terminal tail that precedes the N-terminal domain. This N-terminal tail folds into a helical motif upon recruiting the FimC-subunit complex, but reorganizes into a loop to bind CTD2 during handover. Because both the N-terminal and C-terminal domains of FimD are bound to the end of the growing pilus, the structure further suggests a mechanism for stabilizing the assembly intermediate to prevent the pilus fibre diffusing away during the incorporation of thousands of subunits.
External linksNature / PubMed:30283140 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 5.1 Å
Structure data

EMDB-8953, PDB-6e14:
Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-8954, PDB-6e15:
Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD
Method: EM (single particle) / Resolution: 5.1 Å

Source
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / pili / chaperone / usher

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