B.A., Colby College
Ph.D., Massachusetts Institute of Technology
Postdoctoral Fellow, Lawrence Berkeley National Laboratory, University of California, Berkeley
Areas of Focus:
In the Kung lab, our aim is to gain molecular insight into the function of enzymes by determining and examining their three-dimensional structures. By studying enzyme structures using X-ray crystallography while interrogating their functions with complementary biochemical techniques, we can develop a chemical understanding of enzyme catalysis.
Enzyme systems of particular interest in the Kung lab include those that are involved in producing molecules that are useful to society, such as drug or biofuel compounds. Armed with a deep awareness of how an enzyme’s structure dictates its function, we may even engineer the enzyme in order to alter its function, allowing us to design modified enzymes that are tailor-made to produce more desirable drugs or biofuels.
Ragwan, E.R., Arai, E., and Kung, Y. (2018) New crystallographic snapshots of large domain movements in bacterial HMG-CoA reductase. Biochemistry. DOI: 10.1021/acs.biochem.8b00869. Link.
Miller, B.R. and Kung, Y. (2018) Structural features and domain movements controlling substrate binding and cofactor specificity in class II HMG-CoA reductase. Biochemistry. 57, 654-662. Link.
Kung, Y. and Drennan, C.L. (2017) "One-Carbon Chemistry of Nickel-Containing Carbon Monoxide Dehydrogenase and Acetyl-CoA Synthase" in The Biological Chemistry of Nickel. Eds. Deborah Zamble, Magdalena Rowińska-Żyrek, Henryk Kozlowski. London: Royal Society of Chemistry. pp. 121-148. Link.
Dowling, D.P., Kung, Y., Croft, A.K., Taghizadeh, K., Kelly, W.L., Walsh, C.T., and Drennan, C.L. (2016) Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proc. Natl. Acad. Sci. U.S.A. 113, 12432-12437. Link.
Kung, Y., McAndrew, R.P., Xie, X., Liu, C.C., Pereira, J.H., Adams, P.D., Keasling, J.D. (2014) Constructing tailored isoprenoid products by structure-guided modification of geranylgeranyl reductase. Structure. 22, 1028-1036. Link.
Kung, Y., Ando, N., Doukov, T.I., Blasiak, L.C., Seravalli, J., Bender, G., Ragsdale, S.W., and Drennan, C.L. (2012) Visualizing molecular juggling within a B12-dependent methyltransferase complex. Nature. 48, 265-269. Link.
Kung, Y., Runguphan, W., and Keasling, J.D. (2012) From fields to fuels: Recent advances in the microbial production of biofuels. ACS Synth. Biol. 1, 498-513. Link.
Ando, N., Kung, Y., Can, M., Bender, G., Ragsdale, S.W., and Drennan, C.L. (2012) Transient B12-dependent methyltransferase complexes revealed by small-angle X-ray scattering. J. Am. Chem. Soc. 134, 17945-17954. Link.
Kung, Y. and Drennan, C.L. (2011) A role for nickel-iron cofactors in biological carbon monoxide and carbon dioxide utilization. Curr. Opin. Chem. Biol. 15, 276-283. Link.
Kung, Y., Doukov, T.I., Seravalli, J., Ragsdale, S.W., and Drennan, C.L. (2009) Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry. 48, 7432-7440. Link.