Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate

@inproceedings{Phan2011CrystalSO,
  title={Crystal structure of the FimD usher bound to its cognate FimC:FimH substrate},
  author={Gilles Phan and Han Remaut and Tao Wang and William John Allen and Katharina Franziska Pirker and Andrey Lebedev and Nadine S. Henderson and Sebastian Geibel and Ender Volkan and Jun Biao Yan and Micha B. A. Kunze and Jerome S Pinkner and Bradley A Ford and Christopher W M Kay and Huilin Li and Scott J Hultgren and David G Thanassi and Gabriel Waksman},
  booktitle={Nature},
  year={2011}
}
Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC–FimH chaperone–adhesin complex and that of the unbound form of the FimD translocation domain. The FimD–FimC… CONTINUE READING