We study how proteins function and investigate how they might be modified for new and useful purposes. Our group uses directed evolution to produce mutant proteins which are then screened for enhanced function or other interesting properties. We frequently discover proteins which may be useful in industrial and environmental applications. X-ray crystallography and a variety of other techniques are used to determine the structures of proteins and better understand the detailed mechanics of protein function.
- Liu, J.-W. and Ollis, D.L. (2013). Screening libraries for improved solubility: Using E.coli. Dihydrofolate Reductustase as a reporter. Editor: James Samuelson Publisher: Springer, New York, Methods in Molecular Biology, Volume 97 Enzyme Engineering: Methods and Protocols, Chapter 17, pp. 229-236.
- Stevenson, B.J., Liu, J-W., Kuchel, P.W. and Ollis, D.L. (2012)Fermentative glycolysis with purified Escherichia coli enzymes for in vitro ATP production and evaluating an engineered enzyme. Journal of Biotechnology, 157, pp. 113-123.
- Yip, S. S-C., Foo, J-L., Schenk, G. Gahan, L.R., Carr, P.D. and Ollis D.L. (2011) Directed evolution combined with rational design increases activity of GpdQ towards a non-physiological substrate and alters the oligomeric structure of the enzymeProtein Engineering Design and Selection, 24 pp. 861-872.
- Foo, J-L., Jackson, C.J., Carr, P.D., Kim, H-K., Schenk, G., Gahan, L.R. and Ollis, D.L. (2010). Mutation of outer-shell residues modulates metal ion coordination strength in a metalloenzyme. Biochemical Journal, 429 pp. 313-321.
- Xu, Y., Carr, P.D., Vasudevan, S.G. and David L Ollis (2010) Structure of the adenylylation domain of E. coli Glutamine Synthetase Adenylyltransferase: Evidence for gene duplication and evolution of a new active site. J. Mol. Biol., 396, pp. 773-784.
- Hadler, K., Mitic, N.; Ely, F., Hanson, G., Gahan, L., Larrabee, J., Ollis, D.L., and Schenk, G. (2009) Structural Flexibility enhances the Reactivity of the Bioremediator Glycerophosphodiesterase by Fine-Tuning its Mechanism of Hydrolysis. Journal of the American Chemical Society, 131, pp. 1900-1908.
- Stevenson, B., Liu, J-W. and Ollis, D. Directed evolution of yeast pyruvate decarboxylase 1 for attenuated regulation and increased stability. Biochemistr, 47, pp. 3013-3025.
- Yang, H., Carr, P.D., Yu-McLoughlin, S., Liu, J.W., Horne, I. Qui, X., Jeffries, C.M.J., Russell, R.J., Oakeshott, J.G. and Ollis, D.L. (2003) Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution, Protein engineering, 16, pp. 135-145.
- Carr, P. D., Gustin, S. E., Church, A. P., Murphy, J. M., Ford, S. C., Mann, D. A., Woltring, D. M., Walker, I., Ollis, D. L. and Young, I. G. (2001) Structure of the complete extracellular domain of the common b subunit of the human GM-CSF, IL-3 and IL-5 receptors reveals a novel dimer configuration, Cell, 104, pp. 291-300.
- Jaggi, R., van Heeswijk, W. C., Westerhoff, H. V., Ollis, D. L., and Vasudevan, S. G. (1997) The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction. The EMBO Journal,16, pp. 5562-5571.
- Newcomb, R. D., Campbell, P. M., Ollis, D. L., Cheah, E., Russell, R. J. and Oakeshott, J. G. (1997) A single amino acid substitution converts a carboxylesterase to an organophosporus hydrolase and confers insecticide resistance on a blowfly. Proc. Natl. Acad. Sci. U. S. A., 94, pp. 7464-7468.
- Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., Sussman, J. L., Verschueren, K. H. G. and Goldman, A. (1992) The a/b Hydrolase Fold. Protein Engineering, 5, pp. 197-211.
- Ollis, D.L. and White, S. (1987) The Structural Basis of Protein-Nucleic Acid Interactions, Chemical Reviews, 87 pp. 891-996.
- Ollis, D. L., Kline, C. and Steitz, T. A. (1985) Domain of E. coli DNA Polymerase I Shows Sequence Homology with T7 DNA Polymerase, Nature, 313, pp. 818-819.
- Ollis, D. L., Brick, P., Hamelin, R., Huong, N. G. and Steitz, T. A. (1985) Structure of the Large Fragment of Escherichia coli DNA Polymerase I Complexed with dTMP. Nature, 313, pp. 762-766.