Structural highlights
4j3o is a 5 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Gene: | fimG, b4319, JW4282 (ECOLI), fimH, b4320, JW4283 (ECOLI), fimC, b4316, JW4279 (ECOLI), fimF, b4318, JW4281 (ECOLI), fimD, b4317, JW5780 (ECOLI) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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. [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. [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. [FIMD_ECOLI] Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
Publication Abstract from PubMed
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.
Structural and energetic basis of folded-protein transport by the FimD usher.,Geibel S, Procko E, Hultgren SJ, Baker D, Waksman G Nature. 2013 Apr 11;496(7444):243-6. doi: 10.1038/nature12007. PMID:23579681[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Geibel S, Procko E, Hultgren SJ, Baker D, Waksman G. Structural and energetic basis of folded-protein transport by the FimD usher. Nature. 2013 Apr 11;496(7444):243-6. doi: 10.1038/nature12007. PMID:23579681 doi:http://dx.doi.org/10.1038/nature12007
