Science at the Shine Dome 2010

New Fellows Seminar

Wednesday 5 May

Professor Michael Parker FAA
Biota Structural Biology Laboratory, St Vincent’s Institute of Medical Research

Michael Parker, an Australian Research Council Federation Fellow, is deputy director of St Vincent’s Institute in Melbourne and a professorial fellow at the Bio21 Institute, University of Melbourne. After obtaining his DPhil in protein crystallography from Oxford University, he took up the post of staff scientist at the European Molecular Biology Laboratory in Germany.

In 1991 Michael returned to Australia as a Wellcome Trust Senior Research Fellow to re-establish a protein crystallography laboratory at St Vincent’s. The work of the laboratory is internationally recognised, with the determination of more than 80 crystal structures using synchrotron radiation providing insights into a number of diseases such as cancer, infection and neurological diseases like Alzheimer’s disease. He has published over 200 papers and his work has been recognised with numerous awards, including the 1999 Gottschalk Medal of the Australian Academy of Science.

A tale of two toxins

Pore-forming proteins are produced by many, if not all, organisms. Many of these proteins are toxins that can aid the digestion of prey or can protect the producing organism by killing invaders. At least a third of the more then 300 protein toxins characterised to date act by disrupting the lipid membranes that coat cells. Pore-forming proteins possess the intriguing property that they can exist either in a stable water-soluble state or as an integral membrane pore by undergoing large conformational changes in converting between these two states. Determining the three-dimensional atomic structures of bacterial toxins has made seminal contributions to the fundamental biological question: How can a water-soluble protein insert into or pass through a biological membrane?