Crystallization and preliminary diffraction studies of TraF, a component of the Escherichia coli type IV secretory system

• Author(s) / Creator(s)

  • Manchak, J.
  • Hayakawa, K.
  • Audette, G.F.
  • Holland, S.J.
  • Frost, L.S.
  • Hazes, B.

• TraF, a component of the Escherichia coli type IV secretory system, has been crystallized and preliminary X-ray diffraction data have been collected. TraF is a 26 kDa protein encoded by the E. coli F plasmid and is required for conjugative plasmid transfer and the formation of sex pili. The N-terminal domain of TraF has no recognizable sequence features, whereas the C-terminal domain is believed to adopt a thioredoxin fold. However, since the active-site cysteines of thioredoxin-like proteins are not conserved in TraF, its biochemical role remains unclear. TraF crystallizes in space group C2, with unit-cell parameters a = 119.87, b = 34.36, c = 46.21 A, β= 90.40°, and crystals diffract to 2.3 A resolution.

• Date created

  2004

• Subjects / Keywords

  • Bacteria
  • Proteins
  • Conjugation
  • Plasmids

• Type of Item

  Article (Published)

• DOI

  https://doi.org/10.7939/R3HH6CH1Q

• License

  © 2004 International Union of Crystallography