1TS7

Structure of the pR cis wobble and pR E46Q intermediates from time-resolved Laue crystallography

1TS7 の概要

• エントリーDOI: 10.2210/pdb1ts7/pdb
• 関連するPDBエントリー: 1TS0 1TS6 1TS8
• 分子名称: Photoactive yellow protein, 4'-HYDROXYCINNAMIC ACID (2 entities in total)
• 機能のキーワード: photoreceptor
• 由来する生物種: Halorhodospira halophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14052.73

構造登録者

Ihee, H.,Rajagopal, S.,Srajer, V.,Pahl, R.,Anderson, S.,Schmidt, M.,Schotte, F.,Anfinrud, P.A.,Wulff, M.,Moffat, K. (登録日: 2004-06-21, 公開日: 2005-07-05, 最終更新日: 2017-10-11)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)