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The Crystal Structure Determination of Two Superoxide Dismutases
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Prof. Gary Hunter and Dr Therese  Hunter, from the Department of Physiology and Biochemistry, in collaboration with the Astbury Centre for Structural Molecular Biology, Leeds, UK, have determined the three dimensional structure of two superoxide dismutase proteins (SOD). SOD has many pharmaceutical applications because of its anti-inflammatory and anti-ageing properties

X-ray diffraction data collection was performed at the £st40 million Diamond synchrotron light source, which is nestled like a huge flying saucer in the countryside of Oxfordshire, UK. This was the first such use of the recently inaugurated Diamond facility.

The two SOD proteins used in this study came from the nematode worm Caenorhabditis elegans, an organism studied by many scientists all around the world. More is known about the biology of the worm than about any other animal or plant on the planet. In fact the genome was the first to have its DNA completely sequenced, although the gene, which encodes the SOD-3 protein, was isolated and sequenced in the same laboratory in Malta by Prof. and Dr Hunter, well before the genome sequencing project.

In combination with biochemical and genetic studies, knowing the structure will help us to understand more about the way the protein functions and develop new protein-based pharmaceutical applications for this highly efficient antioxidant. SOD has already been applied to various cosmetics formulations and it has been used as an additive with clot-busting drugs. The human enzyme has been shown to have anti-tumour activity too, an interesting fact as the protein from this study is twice as active as the human version.

Prof. Gary Hunter and Dr Therese Hunter work as a team to study SOD in the Department of Physiology and Biochemistry, Faculty of Medicine and Surgery, University of Malta. SOD is an antioxidant and is responsible for destroying harmful superoxide radicals. All living things, including we humans, make SOD and it is this protein that provides the body with vital protection against this and, as a consequence, other harmful oxygen radicals.

Multidisciplinary scientific techniques were used in order to determine the structure shown. Genetic engineering helped to produce large amounts of the protein, biochemical procedures to purify and crystallise it, then physical operations to expose the crystals to x-rays (using the Diamond facility) and obtain diffraction data. Finally super fast computers with very powerful graphics capabilities turned the diffraction patterns into three-dimensional electron density maps revealing the positions of each heavy atom in the protein. For SOD this amounted to no fewer than 7,446 atoms. This research is the first of its kind to be carried out at the University of Malta.

The structure demonstrates that the worm SODs are incredibly similar to that found in humans. This is important as the worm is used as a model organism to study human diseases. The structure also shows that, at its heart, the protein contains one atom of the metal manganese, essential for the protein to be active and to detoxify oxygen radicals. It is also responsible for the bright pink colour of the protein.

This work was financed by a University of Malta Research Fund to Dr T. Hunter.

Hunter Research 

Aerial Photo courtesy of Diamond Light Source Ltd


Hunter Research


The three-dimensional structure of SOD-3, determined by Prof. Gary Hunter and Dr Therese Hunter, from the University of Malta, in collaboration with Ms Emma Stewart, Dr Chi Trinh and Prof. Simon Phillips of the Astbury Centre for Structural Molecular Biology, Leeds, U.K. The four identical protein chains are shown in different colours, and the non-protein manganese atoms are shown as pink spheres.

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