Structure of the chlamydia trachomatis immunodominant antigen Pgp3

Ahmad Galaleldeen, Alexander B. Taylor, Ding Chen, Jonathan P. Schuermann, Stephen P. Holloway, Shuping Hou, Siqi Gong, Guangming Zhong, P. John Hart

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22 Scopus citations

Abstract

Background: Pgp3 is an immunogenic protein secreted by Chlamydia trachomatis. Results: The trimeric Pgp3 structure reveals globular domains connected by a triple helical coiled-coil. Conclusion: The C-terminal domains resemble tumor necrosis factor, the helical coiled-coil has an unusual twist, and the N-terminal domain is a fusion of virus-like structural motifs. Significance: The Pgp3 structure provides insight into its role in chlamydial pathogenesis.

Original languageEnglish (US)
Pages (from-to)22068-22079
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number30
DOIs
StatePublished - Jul 26 2013

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Galaleldeen, A., Taylor, A. B., Chen, D., Schuermann, J. P., Holloway, S. P., Hou, S., Gong, S., Zhong, G., & Hart, P. J. (2013). Structure of the chlamydia trachomatis immunodominant antigen Pgp3. Journal of Biological Chemistry, 288(30), 22068-22079. https://doi.org/10.1074/jbc.M113.475012