Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1196-201. doi: 10.1107/S1744309113027371. Epub 2013 Oct 26.

Abstract

Chlamydia trachomatis is a major cause of various diseases, including blinding trachoma and pelvic inflammatory disease, and is the leading reported sexually transmitted bacterial infection worldwide. All pathogenic Chlamydiae spp. utilize a supramolecular syringe, or type III secretion system (T3SS), to inject proteins into their obligate host in order to propagate infection. Here, the structure of CT584, a T3SS-associated protein, that has been refined to a resolution of 3.05 Å is reported. The CT584 structure is a hexamer comprised of a trimer of dimers. The structure shares a high degree of similarity to the recently reported structure of an orthologous protein, Cpn0803, from Chlamydia pneumoniae, which highlights the highly conserved nature of this protein across these chlamydial species, despite different tissue tropism and disease pathology.

Keywords: CT584; Chlamydia trachomatis; type III secretion system.

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry*
  • Chlamydia trachomatis / metabolism*
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Protein Multimerization

Substances

  • Bacterial Proteins

Associated data

  • PDB/4MLK
  • PDB/CT584