Biochemistry

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

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

Srivastava D, Schuermann JP, White TA, Krishnan N, Sanyal N, Hura GL, Tan A, Henzl MT, Becker DF, Tanner JJ. Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum. Proc. Natl. Acad. Sci. U. S. A. (2010) 107(7):2878-83.

D. Srivastava, W. Zhu, W.H. Johnson, Jr., C. P.  Whitman, D.F. Becker, and J.J. Tanner. Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N-propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction Biochemistry (2010) 49 (3): 560–569.

Singh H, Schuermann JP, Reilly TJ, Calcutt MJ, Tanner JJ. Recognition of Nucleoside Monophosphate Substrates by Haemophilus influenzae Class C Acid Phosphatase. J. Mol. Biol. (2010) 404(4):639-649.

H. Singh, R.L. Felts, J.P. Schuermann, T.J. Reilly, and J.J. Tanner. Crystal Structures of the Histidine Acid Phosphatase from Francisella tularensis Provide Insight into Substrate Recognition J. Mol. Biol. (2009) 394(5):893-904.

E. L. Ostrander, J.D. Larson, J.P. Schuermann and J.J. Tanner A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate. Biochemistry (2009) 48(5):951-959.

J.J. Tanner Review article: Structural biology of proline catabolism Amino Acids (2008) 35(4), 719-30.

Y. Zhou, J.D. Larson, C.A. Bottoms, E.C. Arturo, M.T. Henzl, J.L. Jenkins, J.C. Nix, D.F. Becker, and J.J. Tanner Structural Basis of Transcriptional Regulation of the Proline Utilization Regulon by Multifunctional PutA J. Mol. Biol. (2008) 381(1):174-88.