Daniel Mattle: How copper leaves the cell

During his studies, Daniel Mattle explored the copper(I) export mechanism of a P-type Cu⁺ ATPase from Legionella pneumophila – a homolog to the human Cu⁺ ATPases. Cu⁺ ATPases are responsible for the homeostatic control of the physiological relevant, but toxic copper(I) cations. To assess the export mechanism of a Cu⁺ ATPase, a combined approach of structural biology and biophysics was choosen to gain a deeper understanding of Cu⁺ binding and export.

The research study indicates a different export mechanism in P-type Cu⁺ ATPases compared to other P-type ATPases and gives insight into the transport mechanism of the disease relevant Cu⁺ ATPases from humans.

The PhD degree was completed at the Section for Structural Biology, Department of Molecular Biolgy and Genetics, Science and Technology, Aarhus University.




Time: Friday 16 August 2013 at 13.15
Place: 1531-113 Aud-D1
Title of dissertation: Structural and functional studies of a Cu⁺ ATPase from Legionella pneumophila
Contact information: Daniel Mattle, e-mail: dmattle@mb.au.dk
Members of the assessment committee:
Professor Werner Kühlbrandt, Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany
Associate Professor Nanna MacAulay, Department of Cellular and Molecular Medicine, University of Kopenhagen
Associate Professor Ditlev E. Brodersen (chair), Department of Molecular Biology and Genetics, Aarhus University
Main supervisor:
Professor Poul Nissen, Department of Molecular Biology and Genetics, Aarhus University
Co-supervisor:
Dr. Pontus Gourdon, Department of Molecular Biology and Genetics, Aarhus University
Dr. Gabriele Meloni, Department of Molecular Biology and Genetics, Aarhus University
Language: The PhD dissertation will be defended in English.

The defence is public.
The dissertation is available for reading at the Graduate School of Science and Technology/GSST, Ny Munkegade 120, building 1521, room 112, 8000 Aarhus C.