| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10870599 | FEBS Letters | 2014 | 7 Pages |
Abstract
HAMP domains are widely abundant signaling modules. The putative mechanism of their function comprises switching between two distinct states. To unravel these conformational transitions, we apply site-directed spin labeling and time-resolved EPR spectroscopy to the phototactic receptor/transducer complex NpSRII/NpHtrII. We characterize the kinetic coupling of NpHtrII to NpSRII along with the activation period of the transducer and follow the transient conformational signal. The observed transient shift towards a more compact state of the HAMP domain upon light-activation agrees with structure-based calculations. It thereby validates the two modeled signaling states and integrates the domain's dynamics into the current model.
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Authors
Daniel Klose, Natalia Voskoboynikova, Ioan Orban-Glass, Christian Rickert, Martin Engelhard, Johann P. Klare, Heinz-Jürgen Steinhoff,