Sequence-specific 1H, 15N, and 13C assignments of the periplasmic chaperone FimC from Escherichia coli.

The periplasmic chaperone FimC is a monomeric, basic 23 kDa protein of 205 amino acid residues (Klemm, 1992) that mediates the assembly of typeI pili in Escherichia coli. Type-I pili are oligomeric protein complexes anchored on the surface of the bacterium and are required for the attachment of E. coli cells to host cell surfaces that are rich in mannose (Klemm, 1992). The determination of the threedimensional structure of FimC should provide novel insights into the mechanism of the chaperone-assisted assembly of bacterial pili on the molecular level.