Structural highlights
Function
[FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC mediates the assembly of type-1 pili, which are filamentous surface organelles of uropathogenic Escherichia coli strains that enable the bacteria to attach to host cell surfaces and persist in macrophages. The availability of the NMR structure of FimC provides a new basis for rational design of drugs against infections by uropathogenic bacteria.
NMR solution structure of the periplasmic chaperone FimC.,Pellecchia M, Guntert P, Glockshuber R, Wuthrich K Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:9783748[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pellecchia M, Guntert P, Glockshuber R, Wuthrich K. NMR solution structure of the periplasmic chaperone FimC. Nat Struct Biol. 1998 Oct;5(10):885-90. PMID:9783748 doi:10.1038/2325
