Structure of a protein photocycle intermediate by millisecond time-resolved crystallography
Structure of a protein photocycle intermediate by millisecond time-resolved crystallography
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DOI：
10.1126/science.275.5305.1471
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发表时间：
1997-03-07
期刊：
影响因子：
56.9
通讯作者：
Getzoff, ED
中科院分区：
文献类型：
--
作者：
Genick, UK;Borgstahl, GEO;Getzoff, ED
蓝光感光器光敏黄蛋白（PYP）经历一个独立的光循环。通过毫秒时间分辨、多波长劳厄晶体学和同步光学光谱法确定了PYP光循环中漂白信号中间体的原子结构。光诱导的反式到顺式异构化的4-羟基肉桂基生色团和耦合蛋白质重排产生一组新的活性位点氢键。精氨酸通道打开，允许溶剂暴露和发色团的酚氧的质子化。蛋白质表面的形状、氢键和静电势的变化形成了信号转导的可能基础。结构的结果提出了一个一般的框架，蛋白质光循环的解释。
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.