Protein Crystallography and Engineering Professor David Ollis

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.

Current research activities

Enzyme engineering

We have determined the structure of an organophosphate degrading enzyme from Agrobacterium radiobacter using crystallographic techniques. Directed evolution is being used to probe the catalytic mechanism of the enzyme. This information may be used to engineer increased enzyme activity and develop improved methods for removal of organophosphate pesticide residues from the environment.

Structure of a molecular editor - the ε Subunit of DNA polymerase III

Checking the DNA strand for errors and correcting them as it is synthesised is essential for the faithful reproduction of genetic information. In bacteria, the machinery to carry out this vital checking process is found in the ε subunit of DNA polymerase III. In order to study the structure and function of this subunit, we have expressed an active and soluble fragment. This has led to the solution of the subunit's X-ray crystal structure. Determining the structure of this protein will enable better understanding of the exact process used to correct errors in DNA synthesis.

Biological regulation - the IL-5 receptor

Interleukin 5 is a regulator of cell growth, differentiation and activation of eosinophils, a type of white blood cell. These cells are of major importance in the body’s response to invasion by parasites and asthma-inducing allergens. We have identified the structure of the ß subunit of the IL-5 receptor and identified residues involved in the binding site. Understanding the interaction between IL-5 and its receptor may enable the development of more effective drugs to induce a faster response to invading allergens.

Annual Research Report   (PDF format)

Group members

Academic Staff:
Professor David Ollis (Leader)     |   Dr Hye-Kyung Kim

Technical and General Staff:
Dr Paul Carr   |   Dr Jian-Wei Liu

PhD Students:
Colin Jackson   |   Bradley Stevenson   |   Morgan Watson

Key publications

1. Xu, Y., Cheah, E., Carr, P.D., van Heeswijk, W.C., Westerhoff, H.V., Vasudevan S.G. and Ollis D.L. GlnK, a P_II - homologue: structure reveals ATP binding site and indicates how the T-loops may be involved in molecular recognition. J.Mol Biol (1998) 282 (1) 149-165.
2. 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. Structure of the complete extracellular domain of the common β subunit of the human GM-CSF, IL-3 and IL-5 receptors reveals a novel dimer configuration. Cell (2001) 104, 291-300.
3. Hamdan, S., Carr, P.D., Brown, S.E., Ollis, D.L., Dixon, N.E. Structural basis for proofreading during replication of the Escheria coli chromosome. Structure with folding and design (2002) 10, 535-546.
4. 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. Evolution of an organophosphate-degrading enzyme: a comparison of natural and directed evolution. Protein engineering (2003) 16(2) 135-145.
5. Yu-McLoughlin, S., Jackson, C., Liu, J-W., and Ollis, D.L. Growth of Escherichia coli coexpressing phosphotriesterase and glyceroophosphodiesterase using paraoxon as sole phosphorus source. Applied and Environmental Microbiology (2004), 70 (1) , 404-412 .

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David Ollis obtained his PhD in Chemistry from the University of Sydney. After postdoctoral studies at Yale University, he was appointed to the Faculty of Northwestern Universitty in Chicago. In 1992 he started as a Senior Fellow heading the Protein Crystallography and Engineering Group as part of the Centre for Molecular Structure and Function within the Research School of Chemistry.

group photos

Professor D L Ollis Research School of Chemistry, Building 35 Australian National University Canberra ACT 0200 AUSTRALIA Ph: +61 2 6125 4377 Fx: +61 2 6125 0750 E-mail: ollis@rsc.anu.edu.au