Friday, January 18 at 4:00pm to 5:00pm
A. Paul Schaap Science Center, Auditorium 1000
35 East 12th Street, Holland, MI 49423-3605
"Shake, Rattle, & Roll: Capturing Snapshots of Metalloproteins in Action"
Abstract: Metalloproteins, or proteins that utilize metals to perform their functions, are responsible for a remarkably wide range of catalytic conversions such as the splitting of dinitrogen and in reactions involved in the life cycle of carbon monoxide. To carry out their functions, these proteins often need to be flexible and assume different conformational states, with subunits of the protein swinging back and forth to enable reactants to enter the active site of the protein or products to leave. In this talk, the conformational gymnastics involved in ribonucleotide reduction are considered. Ribonucleotide reductases (RNRs) are metalloenzymes that use
radical-based chemistry to convert ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair. RNRs are targets for cancer chemotherapies and have been proposed to be candidates for antimicrobial therapies due to these key functions. In this talk, I will describe what we have learned about how RNRs shake, rattle, and roll to accomplish their critical cellular function.
Biography: CATHY L. DRENNAN is a professor of Biology and Chemistry at the Massachusetts Institute of Technology, and a professor and investigator with the Howard Hughes Medical Institute. She received an A.B. in chemistry from Vassar College, and after teaching high school science and drama for three years, she returned to graduate school. Drennan received a Ph.D. in biological
chemistry from the University of Michigan, working in the laboratory of the late Professor Martha L. Ludwig. She was also a postdoctoral fellow with Professor Douglas C. Rees at the California Institute of Technology. In 1999, Drennan joined the faculty at the Massachusetts
Institute of Technology, where she has risen through the ranks to full Professor. Her research interests lie at the interface of chemistry and biology, combining X-ray crystallography with cryo-electron microscopy and other biophysical methods in order to “visualize” molecular processes by obtaining snapshots of metalloproteins in action.