A molecular movie at 1.8 Å resolution displays the photocycle of photoactive yellow protein, a eubacterial blue-light receptor, from nanoseconds to seconds

被引:162
作者
Ren, Z
Perman, B
Srajer, V
Teng, TY
Pradervand, C
Bourgeois, D
Schotte, F
Ursby, T
Kort, R
Wulff, M
Moffat, K
机构
[1] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA
[2] Univ Chicago, Consortium Adv Radiat Sources, Chicago, IL 60637 USA
[3] Univ Chicago, Inst Biophys Dynam, Chicago, IL 60637 USA
[4] Inst Biol Struct Jean Pierre Ebel, UMR 9015, F-38027 Grenoble 1, France
[5] European Synchrotron Radiat Facil, F-38043 Grenoble, France
[6] Univ Amsterdam, Bioctr, EC Slater Inst Biochem Res, Dept Microbiol, NL-1018 WS Amsterdam, Netherlands
关键词
D O I
10.1021/bi0107142
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The photocycle of the bacterial blue-light photoreceptor, photoactive yellow protein, was stimulated by illumination of single crystals by a 7 ns laser pulse. The molecular events were recorded at high resolution by time-resolved X-ray Laue diffraction as they evolved in real time, from I ns to seconds after the laser pulse. The complex structural changes during the photocycle at ambient temperature are displayed in a movie of difference electron density maps relative to the dark state. The step critical to entry into the photocycle is identified as flipping of the carbonyl group of the 4-hydroxycinnamic acid chromophore into an adjacent, hydrophobic environment rather than the concomitant isomerization about the double bond of the chromophore tail. The structural perturbation generated at the chromophore propagates throughout the entire protein as a light-induced "protein quake" with its "epicenter" at the carbonyl moiety of the chromophore.
引用
收藏
页码:13788 / 13801
页数:14
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