Protein photosensors are versatile tools for studying ligand-regulated allostery and signaling. Fundamental to these processes is the amount of energy that can be provided by a photosensor to control downstream signaling events. Such regulation is exemplified by the phototropins - plant serine/threonine kinases that are activated by blue light via conserved LOV (light, oxygen and voltage) domains. The core photosensor of oat phototropin 1 is a LOV domain that interacts in a light-dependent fashion with an adjacent α-helix (Jα) to control kinase activity. We used solution NMR measurements to quantify the free energy of the LOV domain-Jα-helix binding equilibrium in the dark and lit states. These data indicate that light shifts this equilibrium by ∼3.8 kcal mol-1, thus quantifying the energy available through LOV-Jα for light-driven allosteric regulation. This study provides insight into the energetics of light sensing by phototropins and benchmark values for engineering photoswitchable systems based on the LOV-Jα interaction.
|Original language||English (US)|
|Number of pages||7|
|Journal||Nature chemical biology|
|State||Published - Aug 2008|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology