Lesa Beamer and Steven Van Doren
Lesa Beamer has studied the complicated, three-dimensional shapes of protein molecules in her laboratory for many years. These studies, done using X-ray crystallography, provide highly detailed, "atomic resolution" images of proteins and other macromolecules. But several years ago, Beamer realized that crystallographic studies could not answer some of the key questions about the enzyme phosphomannomutase/ phosphoglucomutase (PMM/PGM) her lab was studying. So she turned to a colleague in Biochemistry, Steven Van Doren, who specializes in the use of a complementary method, nuclear magnetic resonance (NMR).
Together, Beamer and Van Doren are now using MU's new 800 MHz spectrometer to answer detailed questions about the function of PMM/PGM. In particular, NMR studies will let them characterize molecular "movements", something that X-ray crystallography cannot do. By combining information on enzyme motions from NMR studies with data from other methods, the team hopes to define hidden “connections” or “networks” of residues in PMM/PGM that allow it to perform its catalytic function. PMM/PGM is an enzyme produced by the pathogenic bacterium Pseudomonas aeruginosa, and has relevance to the fields of biotechnology, metabolic engineering and medicine.
Understanding how motions within a molecule can help transmit information across the structure of a protein is a cutting edge area of research. Beamer (PI) and Van Doren (co-PI) were recently awarded a $1.04 million grant from the National Science Foundation to pursue this work.
"I think NSF liked the interdisciplinary team and combination of techniques we proposed for these studies," Beamer said. She thinks that such collaborative efforts are one of the strengths of doing research at MU.