John J. Tanner
Professor of Chemistry
Joint Professor of Biochemistry
E-mail:tannerjj@missouri.edu
Office: 211 Chemistry Building
Mail: Department of Chemistry
125 Chemistry Building
University of Missouri
Columbia, MO 65211
Phone: 573-884-1280
Fax: 573-882-2754
Lab site: http://www.chem.missouri.edu/TannerGroup/tanner.html
Educational background
| Degree | School | Location | Major |
| BS | University of Missouri | Columbia, Mo. | Chemistry |
| PhD | Brown University | Providence, R.I. | Chemistry |
Research description
We study protein structure and its relationships to protein function at the molecular and cellular levels. Common to all of our work is a focus on understanding how biomolecules recognize and engage one another. Biomolecular recognition is important because virtually all of biological chemistry occurs when two or more molecules come together to effect a reaction or to transmit a signal. For example, enzymes must recognize their natural substrates from the myriad of other molecules in living cells, while transcriptional repressors must recognize a specific DNA sequence to control gene expression.
Our main experimental tool is X-ray crystallography, which provides high resolution three-dimensional structures of proteins. We supplement our crytallographic work with a variety of other approaches, including isothermal titration calorimetry, site-directed mutagenesis, kinetics measurements, analytical ultracentrifugation and computational methods. We are also starting to use small angle X-ray scattering to probe protein structure in solution.
Selected publications
Singh H., Felts R.L., Ma L., Malinski T.J., Calcutt M.J., Reilly T.J., Tanner J.J. (2009) Expression, purification and crystallization of class C acid phosphatases from Francisella tularensis and Pasteurella multocida. Acta Crystallogr. F65: 226-31
Ostrander E.L., Larson J.D., Schuermann J.P., Tanner J.J. (2009) A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. Biochemistry 48(5): 951-9
Schuermann J.P., White T.A., Srivastava D., Karr D.B., Tanner J.J. (2008) Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicum. Acta Crystallogr. F64: 949-53
White T.A., Johnson W.H., Whitman C.P., Tanner J.J. (2008) Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine. Biochemistry 47(20): 5573-80
Tanner J.J. (2008) Structural biology of proline catabolism. Amino Acids 35(4): 719-30
Tan A., Tanner J.J., Henzl M.T. (2008) Energetics of OCP1-OCP2 complex formation. Biophys. Chem. 134: 64-71
Henzl M.T., Tanner J.J. (2008) Solution structure of Ca2+-free rat alpha-parvalbumin. Protein Sci. Vol. 17 (3): 431-8