Determining Structure Alteration of Allosterically Inhibited Rv0045c by Transition Metals through Recrystallization

Emily Lawson Butler University
Faculty Sponsor(s): Geoffrey Hoops Butler University, Mark Macbeth Butler University
Rv0045c is an enzyme catalyzing ester hydrolysis of lipids, an essential reaction in maintaining latent Mycobacterium tuberculosis bacteria, which are responsible for causing the detrimental tuberculosis disease. The enzyme's activity supplies energy for this latent infection; thus, inhibiting the enzyme would eliminate this energy reservoir and render the bacteria unable to maintain a latent infection, working to eradicate the disease and making the enzyme a target for tuberculosis medication. The three-dimensional structure of Rv0045c and the ability of divalent metal cations to allosterically inhibit Rv0045c's function are known, but the structural effects of this inhibition, including the inhibition site and overall protein conformational change, are still unknown. Without a complete visualization of the inhibited protein, medication cannot safely and effectively be engineered for the human body to treat the latent infection. By designing suitable mediums for Rv0045c crystal growth, this study worked to optimally crystallize Rv0045c in the presence of zinc and analyze these crystals through x-ray crystallography, providing the data necessary to produce inhibited Rv0045c's three-dimensional structure.
Biochemistry & Molecular Biology
Poster Presentation

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Irwin Library Lower Level