Issue title: From Molecule to Tissue: XII European Conference on the Spectroscopy of Biological Molecules, Bobigny, France, 1–6 September 2007, Part 2 of 2
Affiliations: Institut für Biophysik, Johann Wolfgang Goethe-Universität Frankfurt, 60438 Frankfurt, Germany
Note: [] Corresponding author: K. Hauser, Institut für Biophysik, Johann Wolfgang Goethe-Universität Frankfurt, Max-von-Laue-Str. 1, 60438 Frankfurt, Germany. Tel.: +49 69 798 46407; Fax: +49 69 798 46 423; E-mail: hauser@biophysik.uni-frankfurt.de.
Abstract: P-type ATPases are membrane proteins acting as ion pumps that drive an active transport of cations across the membrane against a concentration gradient. The required energy for the ion transport is provided by binding and hydrolysis of ATP. A reaction mechanism of ion transport and energy transduction is assumed to be common for all P-type ATPases and generally described by the Post-Albers cycle. Transient currents and charge translocation of P-type ATPases were extensively investigated by electrical measurements that apply voltage jumps to initiate the reaction cycle. In this study, we simulate an applied voltage across the membrane by an electric field and perform electrostatic calculations in order to verify the experimentally-driven hypothesis that the energy transduction mechanism is regulated by specific structural elements. Side chain conformational and ionization changes induced by the electric field are evaluated for each transmembrane helix and the selectivity in response is qualitatively analyzed for the Ca2+-ATPase as well as for structural models of the Na+/K+-ATPase. Helix M5 responds with more conformer changes as compared to the other transmembrane helices what is even more emphasized when the stalk region is included. Thus our simulations support experimental results and indicate a crucial role for the highly conserved transmembrane helix M5 in the energy transduction mechanism of P-type ATPases.
Keywords: P-type ATPase, energy transduction, transport, electric field, electrostatics
DOI: 10.3233/SPE-2008-0343
Journal: Spectroscopy, vol. 22, no. 4, pp. 319-325, 2008
