Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds

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Determining 3D intermediate structures during the biological action of proteins in real time under ambient conditions is essential for understanding how proteins function. Here we use timer-esolved Laue crystallography to extract short-lived intermediate structures and thereby unveil signal transduction in the blue light photoreceptor photoactive yellow protein (PYP) from Halorhodospira halophila. By analyzing a comprehensive set of Laue data during the PYP photocycle (forty-seven time points from one nanosecond to one second), we track all atoms in PYP during its photocycle and directly observe how absorption of a blue light photon by its p-coumaric acid chromophore triggers a reversible photocycle. We identify a complex chemical mechanism characterized by five distinct structural intermediates. Structural changes at the chromophore in the early, red-shifted intermediates are transduced to the exterior of the protein in the late, blue-shifted intermediates through an initial "volume-conserving" isomerization of the chromophore and the progressive disruption of hydrogen bonds between the chromophore and its surrounding binding pocket. These results yield a comprehensive view of the PYP photocycle when seen in the light of previous biophysical studies on the system.
Publisher
NATL ACAD SCIENCES
Issue Date
2005-05
Language
English
Article Type
Article
Keywords

P-COUMARIC ACID; ECTOTHIORHODOSPIRA-HALOPHILA; PHOTORECEPTOR PROTEIN; PHOTOCYCLE INTERMEDIATE; PHOTOTROPHIC BACTERIUM; ANGSTROM RESOLUTION; STRUCTURAL-CHANGES; E46Q MUTANT; CHROMOPHORE; KINETICS

Citation

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.102, no.20, pp.7145 - 7150

ISSN
0027-8424
DOI
10.1073/pnas.0409035102
URI
http://hdl.handle.net/10203/250827
Appears in Collection
CH-Journal Papers(저널논문)
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