Open AccessStructure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution
Author(s) -
Barta Michael L.,
Hickey John,
Kemege Kyle E.,
Lovell Scott,
Battaile Kevin P.,
Hefty P. Scott
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113027371
Subject(s) - chlamydiae , chlamydia trachomatis , biology , chlamydia , pelvic inflammatory disease , obligate , virology , microbiology and biotechnology , trachoma , immunology , medicine , pathology , ecology , gynecology
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.