Cellular processes responsible for life as we know it are dependent on metal atoms. Research in the Colbert Laboratory focuses on the molecular mechanisms of metal trafficking. Specifically, how do bacteria import and utilize iron in key cellular processes. Understanding these molecular mechanisms will further our knowledge of bacterial survival not only in the wild, but also during pathogenesis. We use a combination of structural (X-ray crystallography and NMR spectroscopy) and biochemical techniques (protein chromatography, mutagenesis, spectroscopy, etc.) to address basic questions concerning the mechanisms by which proteins facilitate and regulate the import and utilization of iron in cells. This fundamental information will provide key information in designing not only novel therapeutics toward antibiotic resistant strains of bacteria, but will also underlie our basic understanding of human diseases involved in erroneous metal trafficking.
Colbert, C. L., Chai-Wan Kim , Young-Ah Moon , Lisa Henry , Maya Palnitkar , William McKean , Kevin Fitzgerald , Johann Deisenhofer, Jay Horton , Hyock Joo Kwon. (2010). The Crystal Structure of Spot14, a Modulator of Fatty Acid Synthesis. Proc Natl Acad Sci USA 107, 18820-18825.
Sinha, S. C., Colbert, C. L., Becker, N., and Levine, B. (2008). Molecular mechanism of the inhibition of Beclin 1-dependent autophagy by the γ-herpesviridae. Autophagy 4, 989-997 (Cover)
Huang, Y., Baxter, R., Smith, B. S., Partch, C. L., Colbert, C. L., and Deisenhofer, J. (2006). Crystal structure of cryptochrome 3 from Arabiopsis thaliana and its implications for photolyase activity. Proc Natl Acad Sci USA 103, 17701-17706.
Colbert, C. L., Wu, Q., Erbel, P. J. A., Gardner, K. H., and Deisenhofer, J. (2006). Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation. Proc Natl Acad Sci USA 103, 4410-4415.
Couture, M. M.-J., Colbert, C. L., Babini, E., Rosell, F. I., Mauk, A. G., Bolin, J. T., and Eltis L. D. (2001). Characterization of BphF, a Rieske-Type Ferrodoxin with a Low Reduction Potential. Biochemistry 40, 84-92.
Colbert, C. L., Couture, M. M.-J., Eltis, L. D., and Bolin, J. T. (2000). A Cluster Exposed: Structure of the Rieske Ferrodoxin from Biphenyl Dioxygenase and the Redox Properties of Rieske Fe-S Proteins. Structure 8, 1267-1278.
Imbeault, N. Y. R., Powlowski, J. B., Colbert, C. L., Bolin, J. T., and Eltis, L. D. (2000). Steady-state Kinetic Characterization and Crystallization of a PCB-Transforming Dioxygenase. J Biol Chem 275, 12430-12437.
Zauhar, R. J., Colbert, C. L., Morgan, R. S., and Welsh, W. (2000). Evidence for a Strong Sulfur-Aromatic Interaction Derived from Crystallographic Data. Biopolymers 53, 233-248.