Structural and Biochemical Characterization of Chlamydia trachomatis Hypothetical Protein CT263 Supports That Menaquinone Synthesis Occurs through the Futalosine Pathway

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Issue Date
2014-09-24Author
Barta, Michael L.
Thomas, Keisha
Yuan, Hongling
Lovell, Scott
Battaile, Kevin P.
Schramm, Vern L.
Hefty, P. Scott
Publisher
American Society for Biochemistry and Molecular Biology
Type
Article
Article Version
Scholarly/refereed, publisher version
Rights
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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Show full item recordAbstract
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.
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Citation
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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