Regensburg 2010 – wissenschaftliches Programm
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BP: Fachverband Biologische Physik
BP 29: Biomolecular Spectroscopy
BP 29.4: Vortrag
Donnerstag, 25. März 2010, 15:15–15:30, H45
Conformation studies of the gram-negative-bacteria protein TonB by pulse EPR — •Silvia Domingo Köhler1, Annemarie Weber2, Wolfram Welte2, and Malte Drescher1 — 1Department of Chemistry, University of Konstanz, 78457 Konstanz, Germany — 2Department of Biology, University of Konstanz, 78457 Konstanz, Germany
To transport Iron complexed in ferric siderophores through the outer membrane of gram-negative bacteria energy is required. It is proposed that a complex composed in particular by the TonB protein and anchored in the inner membrane opens channels in the outer membrane. The energy needed is only available in the inner membrane, in form of the proton motive force. Structure and dynamics of the protein TonB plays a key role in unraveling how the energy is transferred to the outer membrane, in order to induce a conformational change in the outer membrane receptors. However, the structure of TonB is not completely determined and the mechanism of energy transduction remains still unclear.
To unravel structure and functionality of TonB site-directed spin-labeling in combination with pulsed electron paramagnetic resonance (EPR) techniques is an outstandingly suitable tool. Determining conformation and conformational changes of TonB helps to elucidate a mechanism which has general implications for signal transduction within and between proteins.