PMID:9783748

Citation	Pellecchia, M, Güntert, P, Glockshuber, R and Wüthrich, K (1998) NMR solution structure of the periplasmic chaperone FimC. Nat. Struct. Biol. 5:885-90
Abstract	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.
Links	PubMed Online version:10.1038/2325
Keywords	Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Proteins; Consensus Sequence; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins; Fimbriae Proteins; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Protein Structure, Tertiary
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.