| Structural highlights6e15 is a 5 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Gene: | fimC, b4316, JW4279 ("Bacillus coli" Migula 1895), fimD_3, APZ14_00735, AW106_26365, COD30_02575, CXB56_24500, ERS085374_04437, ERS150876_04614, FORC28_5312 ("Bacillus coli" Migula 1895), fimF, b4318, JW4281 ("Bacillus coli" Migula 1895), fimG, b4319, JW4282 ("Bacillus coli" Migula 1895), fimH, b4320, JW4283 ("Bacillus coli" Migula 1895) |
| Experimental data: | Check | | Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function[FIMG_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH. [FIMF_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae. [FIMH_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
Publication Abstract from PubMed
Pathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors(1). Type 1 pili are assembled via the conserved chaperone-usher pathway(2-5). 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 beta-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.
Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD.,Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, Li H Nature. 2018 Oct 3. pii: 10.1038/s41586-018-0587-z. doi:, 10.1038/s41586-018-0587-z. PMID:30283140[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See AlsoReferences
- ↑ Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, Li H. Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD. Nature. 2018 Oct 3. pii: 10.1038/s41586-018-0587-z. doi:, 10.1038/s41586-018-0587-z. PMID:30283140 doi:http://dx.doi.org/10.1038/s41586-018-0587-z
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