An atomic resolution model for assembly, architecture, and function of the Dr adhesins

Mol Cell. 2004 Aug 27;15(4):647-57. doi: 10.1016/j.molcel.2004.08.003.


Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adhesins, Escherichia coli / chemistry*
  • Adhesins, Escherichia coli / genetics
  • Adhesins, Escherichia coli / metabolism
  • Amino Acid Sequence
  • CD55 Antigens / chemistry
  • CD55 Antigens / metabolism
  • Crystallography, X-Ray
  • Escherichia coli / chemistry*
  • Escherichia coli / metabolism
  • Escherichia coli / pathogenicity
  • Fimbriae, Bacterial
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Tertiary*
  • Protein Subunits / chemistry
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Sequence Alignment
  • Surface Plasmon Resonance


  • Adhesins, Escherichia coli
  • CD55 Antigens
  • Protein Subunits

Associated data

  • PDB/1RXL