Our lab is actively involved in three-dimensional structure characterization of macromolecules using X-ray crystallography as a primary tool, with an increasing emphasis on functional studies. We apply crystallographic, biophysical, biochemical and cell biology methods to study several classes of biologically important proteins. Current projects focus on kinases and phosphatases, effector proteins involved in pathogen-host interaction as well as proteins implicated in bacterial pathogenicity.
Protein crystallography is a powerful tool capable of revealing atomic details of protein. The technique has been widely used to determine 3-D structures of proteins, multi-domain large protein complexes, protein-DNA interactions etc. Protein crystallography has in the last decade advanced greatly and made a major contribution to the fundamental understanding of biological processes and provided insights into problems of molecular recognition and biological control of importance to medicine and the pharmaceutical industry. Our research, currently focusing on structure-function studies of a number of biologically significant proteins, is largely funded by Canadian Institutes of Health Research (CIHR) and Natural Sciences and Engineering Research Council of Canada (NSERC). Please visit our lab website to find out more.
Phosphatases/kinases are involved in a wide range of cellular processes. We are working on a number of novel bacterial kinases and phosphatase. Along with structural characterization, we are also interested in probing their cellular and biochemical function by using a wide variety of approaches including cell biology, biochemical and biophysical methods.
Bacterial structure genomics provides us with an opportunity to systematically study a selected group of protein. We are particularly interested in proteins with "unknown" function and protein-protein complex structures, as well as those involved in pathogen-host interactions. Based on the structural insights, we hope to obtain important clues for the function, and subsequently verify it by biochemical experiments.
- C. Prince and Z. Jia. (2015) An unexpected duo: Rubredoxin binds nine TPR motifs to form LapB, an essential regulator of lipopolysaccharide synthesis. Structure, 23, 1500-1506.
- W. Wu, M.N. Rahman, J. Guo, N. Roy, L. Xue, C.M. Cahill, S. Zhang and Z. Jia. (2015) Otoferlin-GAD65 coupling and its effects on GABAergic activity. J. Mol. Cell Biol. 7, 168-179.
- L.M. van Staalduinen, F.R. McSorley, K. Schiessl, J. Séguin, P.B. Wyatt, F. Hammerschmidt, D.L. Zechel and Z. Jia. (2014) The crystal structure of PhnZ in complex with substrate reveals a new di-iron oxygenase mechanism for catabolism of organophosphonates. Proc. Natl. Acad. Sci. 111, 5171-5176.
- J. Zheng and Z. Jia. (2013) Tiny enzyme uses context to succeed. Nature, 497, 445-446.
- C. Prince and Z. Jia. (2012) Measurement of detergent concentration using 2,6-dimethylphenol in membrane-protein crystallization. Acta Cryst. D68, 1694-1696.
- J. Zheng and Z. Jia. (2010) Structure of the bifunctional isocitrate dehydrogenase kinase/phosphatase. Nature, 465, 961-965.
- B. Wathen and Z. Jia. (2010) Protein beta-sheet nucleation is driven by local modular formation. J. Biol. Chem. 285, 18376-18384.
- Q. Ye, S.W. Crawley, Y. Yang, G.P. Côté and Z. Jia. (2010) Crystal structure of the alpha-kinase domain of Dictyostelium myosin heavy chain kinase A. Sci. Signal. 3, ra17.
- D. Lee and Z. Jia. (2009) Emerging structural insights into bacterial tyrosine kinases. Trends Biochem. Sci. 34, 351-357.
- D. Lee, J. Zheng, Y.-M. She and Z. Jia. (2008) Structure of Escherichia coli tyrosine kinase Etk reveals novel activation mechanism. EMBO J. 27, 1758-1766.