Lesa J. Beamer

Associate Professor of Biochemistry

Email:	beamerl@missouri.edu
Phone:	(573) 882-6072
Lab:	(573) 884-2302
Fax:	(573) 884-4812
Office:	105A Schlundt Annex
Mailing Address:	Biochemistry 117 Schweitzer Hall University of Missouri-Columbia Columbia, MO 65211
Research Areas:	Structural biology: X-ray crystallography of medically important proteins.

Educational Background

BS		Kent State University	Kent, Ohio	Chemistry
PhD		Johns Hopkins School of Medicine	Baltimore, Md.	Biochemistry

Notable Honors and Service

Chair, BIOMAC Special Interest Group American Crystallographic Association
Program Director, 2004 Annual meeting of the American Crystallographic Association

Research Description

Our laboratory studies the three-dimensional structures of proteins relevant to human disease. A major focus of the lab is characterizing bacterial enzymes important to the virulence of infections. Bacterial polysaccharides are often critical determinants of infectivity, and therefore the enzymes involved in carbohydrate biosynthesis are excellent targets for antimicrobial agents. One enzyme family of interest to us is the alpha-D-phosphohexomutase family. These enzymes catalyze the production of phosphorylated sugar precursors that are assembled in more complex carbohydrates. Our laboratory has characterized a protein in one sub-group of the family, the enzyme PMM/PGM from P. aeruginosa. We are currently studying other enzymes in the family from important human pathogens, including B. anthracis, S. aureus, and V. cholerae, using X-ray crystallography and bioinformatic methods. We seek to understand the relationships between protein structure, kinetic mechanisms, and sequence relationships in the family, to facilitate the design of clinical inhibitors. In addition, we are characterizing the role of protein dynamics is the mechanism of P. aeruginosa PMM/PGM via NMR techniques, in collaboration with the laboratory of Dr. Steven Van Doren.

For more info on our research program, see the MU Structural Biology homepage.

Selected Publications

Regni, C., Shackelford, G.S., and Beamer, L.J. Complexes of the enzyme PMM/PGM with a slow substrate and inhibitor, Acta Cryst. (2006). F62, 722-726

Regni, C.A., Schramm, A.M., and Beamer, L.J. The reaction of phosphohexomutase from P. aeruginosa: Structural insights into a simple processive enzyme, J. Biol. Chem. 281: 15564-15571 (2006).

Lo, S.-C., Li, X., Henzl, M., Beamer, LJ and Hannink M. analysis of the Keap1:Nrf2 interface reveals a novel mechanism for substrate binding to substrate adaptor proteins, EMBO 25: 3605-3617 (2006).

Beamer, L.J., Li, X., Bottoms, C.A., and Hannink, M. Conserved solvent and side chain structural interactions in the 1.35 Å structure of the Kelch domain of Keap1. Acta Cryst. (2005). D61, 1335-1342.

Li, X., Zhang, D., Hannink, M., and Beamer, L.J. Crystal structure of the Kelch domain of Keap1, J. Biol. Chem. 279: 54750-54758 (2004).

Evolutionary trace analysis of the α-D-phosphohexomutase superfamily. Shackelford, G.S., Regni, C.A., and Beamer, L.J. Protein Science 13:2130-2138 (2004).

Regni, C., Naught, L.E., Tipton, P.A., Beamer, L.J. Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa, Structure 12: 55-63 (2004).

Employment Opportunities

Post-Doctoral Opportunities

Electronic submission is encouraged, e-mail to biochemsearch@missouri.edu

Applicants should send CV and names of two references to:
Dr. Lesa Beamer
Postdoctoral Application
Biochemistry
117 Schweitzer Hall
University of Missouri-Columbia
Columbia, MO 65211

Structural biology: X-ray crystallography of medically important proteins.