1TS0

Structure of the pB1 intermediate from time-resolved Laue crystallography

Summary for 1TS0

• Entry DOI: 10.2210/pdb1ts0/pdb
• Related: 1TS6 1TS7 1TS8
• Descriptor: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (2 entities in total)
• Functional Keywords: photoreceptor
• Biological source: Halorhodospira halophila
• Total number of polymer chains: 1
• Total formula weight: 14052.73

Authors

Ihee, H.,Rajagopal, S.,Srajer, V.,Pahl, R.,Anderson, S.,Schmidt, M.,Schotte, F.,Anfinrud, P.A.,Wulff, M.,Moffat, K. (deposition date: 2004-06-21, release date: 2005-07-05, Last modification date: 2025-03-26)

Primary citation

Ihee, H.,Rajagopal, S.,Srajer, V.,Pahl, R.,Anderson, S.,Schmidt, M.,Schotte, F.,Anfinrud, P.A.,Wulff, M.,Moffat, K.
Visualizing reaction pathways in photoactive yellow protein from nanoseconds to seconds.
Proc.Natl.Acad.Sci.Usa, 102:7145-7150, 2005

PubMed Abstract: 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 time-resolved 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.

PubMed: 15870207
DOI: 10.1073/pnas.0409035102

Experimental method

X-RAY DIFFRACTION (1.6 Å)