Abstract
The phytochrome family of light-switchable proteins has long been studied by biochemical, spectroscopic and crystallographic means, while a direct probe for global conformational signal propagation has been lacking. Using solution X-ray scattering, we find that the photosensory cores of several bacterial phytochromes undergo similar large-scale structural changes upon red-light excitation. The data establish that phytochromes with ordinary and inverted photocycles share a structural signaling mechanism and that a particular conserved histidine, previously proposed to be involved in signal propagation, in fact tunes photoresponse.
Original language | English |
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Pages (from-to) | 3379-3383 |
Journal | The Journal of Physical Chemistry Letters |
Volume | 6 |
Issue number | 17 |
DOIs | |
Publication status | Published - 2015 |
Subject classification (UKÄ)
- Biochemistry and Molecular Biology