Structural and Biochemical Characterization of Chlamydia trachomatis Hypothetical Protein CT263 Supports That Menaquinone Synthesis Occurs through the Futalosine Pathway
Barta, Michael L.
Battaile, Kevin P.
Schramm, Vern L.
Hefty, P. Scott
American Society for Biochemistry and Molecular Biology
Scholarly/refereed, publisher version
This research was originally published in Journal of Biological Chemistry. Michael L. Barta, Keisha Thomas, Hongling Yuan, Scott Lovell, Kevin P. Battaile‖, Vern L. Schramm and P. Scott Hefty. Structural and Biochemical Characterization of Chlamydia trachomatis Hypothetical Protein CT263 Supports That Menaquinone Synthesis Occurs through the Futalosine Pathway. Journal of Biological Chemistry. 2014; 289: 32214-32229. © the American Society for Biochemistry and Molecular Biology.
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BACKGROUND: Specific pathways and components for respiration in Chlamydia are poorly understood. RESULTS: The C. trachomatis hypothetical protein CT263 crystal structure displays strong structural similarity with 5′-methylthioadenosine nucleosidase enzymes. CONCLUSION: Bioinformatic analyses and enzymatic characterization of CT263 suggest menaquinone biosynthesis proceeds through the futalosine pathway in Chlamydiaceae. SIGNIFICANCE: Unique structural aspects of the CT263 active site can be leveraged to modify existing transition state inhibitors.
Barta, M. L., Thomas, K., Yuan, H., Lovell, S., Battaile, K. P., Schramm, V. L., & Hefty, P. S. (2014). Structural and biochemical characterization of Chlamydia trachomatis hypothetical protein CT263 supports that menaquinone synthesis occurs through the futalosine pathway. Journal of Biological Chemistry, 289(46), 32214-32229.
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