3D structure of EspA filaments from enteropathogenic Escherichia coli

Mol Microbiol. 2003 Jul;49(2):301-8. doi: 10.1046/j.1365-2958.2003.03555.x.


The type III secretion system (TTSS) is a modular apparatus assembled by many pathogenic Gram-negative bacteria and is designed to translocate proteins through the bacterial cell wall into the eukaryotic host cell. The conserved components of the TTSS comprise stacks of rings spanning the inner and outer bacterial membrane and a narrow, needle-like structure projecting outwards. The TTSS of enteropathogenic E. coli is unique in that one of the translocator proteins, EspA, polymerizes to form an extension to the needle complex which interacts with the host cell. In this study we present the 3D structure of EspA filaments to c. 26 A resolution determined from electron micrographs of negatively stained preparations by image processing. The structure comprises a helical tube with a diameter of 120 A enclosing a central channel of 25 A diameter through which effector proteins may be transported. The subunit arrangement corresponds to a one-start helix with 28 subunits present in five turns of the helix and an axial rise of 4.6 A per subunit. This is the first report of a 3D structure of a filamentous extension to the TTSS.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Escherichia coli / chemistry*
  • Escherichia coli / metabolism*
  • Escherichia coli / pathogenicity
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Escherichia coli Proteins / ultrastructure
  • Flagella / chemistry
  • Fourier Analysis
  • Humans
  • Image Processing, Computer-Assisted
  • Models, Molecular
  • Protein Structure, Tertiary*
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism


  • Escherichia coli Proteins
  • EspA protein, E coli
  • Protein Subunits