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 |
|---|---|
| Pages (from-to) | 3379-3383 |
| Number of pages | 5 |
| Journal | Journal of Physical Chemistry Letters |
| Volume | 6 |
| Issue number | 17 |
| DOIs | |
| Publication status | Published - 3 Sept 2015 |
Keywords
- phytochromes
- protein dynamics
- signal transduction
- X-ray scattering