Anti-malarials and biological batteries:
The first membrane protein structure solved in Finland

As a first in Finland, an Institute of Biotechnology research group has solved a membrane protein structure. Sodium pumping pyrophosphatases may in the future be part of biological battery systems. Solving the structure might also help fighting malaria and other diseases caused by protozoa.

Professor Adrian Goldman and his group at the Institute of Biotechnology, University of Helsinki, has solved the structure of an integral membrane protein for the first time in Finnish science history. The protein, sodium pumping pyrophosphatase, sits in the cell membrane and pumps ions from one side of the membrane to the other. The research was funded by the Academy of Finland.

“The energy for pumping is taken from pyrophosphate, which can be produced industrially at reasonable cost. Sodium pumping pyrophosphatases may thus in the future be part of biological batteries, research director Adrian Goldman predicts.

Membrane-bound pyrophosphatases cannot be found in humans but they are very important for plant development. Protozoan parasites too, like the malaria parasite, have the same enzymes. The protein structure will help us designing specific drugs to disturb its function.

“Membrane proteins in general are important targets for drugs. About 60 percent of all drugs work by attaching themselves to membrane proteins”, says researcher Juho Kellosalo from the same research group.

The sodium pumping pyrophosphatase comes from Thermotoga maritima, a bacterium living in marine hydrothermal vents and hot springs. The structure was solved by x-ray crystallography.  Purified protein was crystallised and the crystals bombarded with powerful x-rays. That way the protein structure could be understood down to the level of each atom in the protein. The researchers also used it to develop a picture of how the sodium pumping occurs.

Science 27th July 2012: The structure and catalytic cycle of a sodium pumping pyrophosphatase. Authors: Juho Kellosalo (1,2), Tommi Kajander (1), Konstantin Kogan (1), Kisun Pokharel (1,3), Adrian Goldman (1)

1 Structural Biology and Biophysics Program, Institute of Biotechnology, University of Helsinki
2 Graduate School of Informational and Structural Biology
3 Department of Biochemistry and Food Chemistry, University of Turku

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