Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution

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Issue Date
2013-10-05Author
Barta, Michael L.
Hickey, John M.
Kemege, Kyle Evan
Lovell, Scott
Battaile, Kevin P.
Hefty, P. Scott
Publisher
International Union of Crystallography
Type
Article
Article Version
Scholarly/refereed, publisher version
Rights
Copyright © International Union of Crystallography 2013
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Show full item recordAbstract
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.
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Citation
Barta, M. L., Hickey, J., Kemege, K. E., Lovell, S., Battaile, K. P., & Hefty, P. S. (2013). Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(Pt 11), 1196–1201. http://doi.org/10.1107/S1744309113027371
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