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Structural and Biochemical Characterization of Chlamydia trachomatis Hypothetical Protein CT263 Supports That Menaquinone Synthesis Occurs through the Futalosine Pathway
Barta, Michael L. Thomas, Keisha Yuan, Hongling Lovell, Scott Battaile, Kevin P. Schramm, Vern L. Hefty, P. Scott
Barta, Michael L.
Thomas, Keisha
Yuan, Hongling
Lovell, Scott
Battaile, Kevin P.
Schramm, Vern L.
Hefty, P. Scott
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Abstract
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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Date
2014-09-24
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American Society for Biochemistry and Molecular Biology
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Research Projects
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Keywords
Chlamydia, Crystallography, Enzyme Kinetics, Quinone, Respiration
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.