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Structure and Dynamics of Enzyme-Ligand Interactions

Prof. Katherine Davis, guest speaker
Prof. Katherine Davis
Assistant Professor, Department of Chemistry
Emory University
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Inorganic Seminar

Essential across all domains of life, enzymes often expedite challenging biological reactions by incorporating transition metal ions whose oxidation and spin states are coordinated with changes in atomic structure. While great strides have been made in the field of metalloenzymology, our understanding of these dynamic processes remains limited as the timescales on which they occur render visualization technically challenging. In this talk, I will describe the time-resolved X-ray methods my group is developing to elucidate both local electronic changes to the metal center, as well as global structural motions, that enable reactivity of metal-containing enzymes, in particular, those important for human health and medicine. While these approaches are under development, we have employed computational methods together with cryo-crystallography to interrogate the substrate binding modes of two key enzymes produced by pathogenic bacteria. The first project provides insights into the inhibition of the drug target dihydroorotate dehydrogenase by bacterial hydroxyalkylquinolines, while the second attempts to elucidate the role of a putative substrate-binding domain associated with the biosynthesis of ribosomally synthesized and posttranslationally modified peptides.

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