Structural and functional studies of a Cu+-ATPase from Legionella pneumophila

Publikation: Bog/antologi/afhandling/rapportPh.d.-afhandlingForskning

  • Daniel Mattle, Danmark
During his studies, Daniel Mattle explored the copper(I) export mechanism of a P-type Cu+ ATPase from Legionella pneumophila – a homologue 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, Daniel Mattle chose a combined approach of structural biology and biophysics to gain a deeper understanding of Cu+ binding and export.
The research study indicates a different export mechanism in P-type Cu+ ATPases compared with other P-type ATPases and provides insight into the transport mechanism of the disease-relevant Cu+ ATPases from humans.
OriginalsprogEngelsk
ForlagAarhus University, Faculty of Science and Technology
Rekvirerende organGraduate School of Science and Technology
StatusUdgivet - 2013

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Denfence on 16th August 2013

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