NMR SOLUTION STRUCTURE OF THE PERIPLASMIC CHAPERONE FIMC

The NMR structure of the 205-residue periplasmic chaperone FimC is pre sented. This protein consists of two globular domains with immunoglobu lin-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 pill, 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 infecti ons by uropathogenic bacteria.