Fimbriae and pili are macromolecular structures on the surface of Gram negative bacteria that are important for cellular adhesion. A 2.7 angstrom resolution crystal structure of a complex of Escherichia coil fimbrial proteins containing FimH, FimG, FimF, and FimC provides the most complete model to date for the arrangement of subunits assembled in the native structure. The first three proteins form the tip of the fimbriae while FimC is the chaperone protein involved in the usher/chaperone assembly process. The subunits interact through donor strand complementation where a beta-strand from a subunit completes the beta-sandwich structure of the neighboring subunit or domain closer to the tip of the fimbria. The function of FimC is to provide a surrogate donor strand before delivery of each subunit to the FimD usher and the growing fimbria. Comparison of the subunits in this structure and their chaperone-bound complexes show that the two FimH domains change their relative orientation and position in forming the tip structure. Also, the non-chaperone subunits undergo a conformational change in their first beta-strand when the chaperone is replaced by the native donor strand. Some residues move as much as 14 angstrom in the process. This structural shift has not been noted in structural studies of other bacterial adhesion sub-structures assembled via donor strand complementation. The domains undergo a significant structural change in the donor strand binding groove during fimbrial assembly, and this likely plays a role in determining the specificity of subunit-subunit interactions among the fimbrial proteins. (C) 2010 Elsevier Inc. All rights reserved.