Mechanisms of membrane transport visualized by electron microscopy and x-ray crystallography

Research report (imported) 2006 - Max Planck Institute of Biophysics

Kühlbrandt, Werner; Appel, Matthias; Barton, Bastian; Kalthoff, Christoph; Raunser, Stefan; Schröder, Rasmus; Vinothkumar, Kutti Ragunath; Yildiz, Özkan
Strukturbiologie (Prof. Dr. Werner Kühlbrandt)
MPI für Biophysik, Frankfurt am Main
In recent research the Department of Structural Biology at the Max Planck Institute of Biophysics addressed membrane transport proteins from thermophilic archaea, which are more robust than their eukaryotic counterparts yet often quite similar to them, and thus serve as good models for medically relevant systems. They determined the structure of a signaling protein that regulates nitrogen uptake in archaea and bacteria in three different states, which helped them to elucidate the regulatory mechanism. Furthermore they investigated pH- and ion-induced conformational changes that accompany activation and ion transport in sodium-proton exchange proteins, and in the outer membrane porin OmpG from E. coli.

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