Structure of a protein photocycle intermediate by millisecond time-resolved crystallography
- Scripps Research Institute, La Jolla, CA (United States); and others
The blue-light photoreceptor photoactive yellow protein (PYP) undergoes a self-contained light cycle. The atomic structure of the bleached signaling intermediate in the light cycle of PYP was determined by millisecond time-resolved, multiwavelength Laue crystallography and simultaneous optical spectroscopy. Light-induced trans-to-cis isomerization of the 4-hydroxycinnamyl chromophore and coupled protein rearrangements produce a new set of active-site hydrogen bonds. An arginine gateway opens, allowing solvent exposure and protonation of the chromophore`s phenolic oxygen. Resulting changes in shape, hydrogen bonding, and electrostatic potential at the protein surface form a likely basis for signal transduction. The structural results suggest a general framework for the interpretation of protein photocycles. 31 refs., 4 figs., 2 tabs.
- OSTI ID:
- 467957
- Journal Information:
- Science, Journal Name: Science Journal Issue: 5305 Vol. 275; ISSN SCIEAS; ISSN 0036-8075
- Country of Publication:
- United States
- Language:
- English
Similar Records
Watching a signaling protein function in real time via 100-ps time-resolved Laue crystallography