Seeing the light with BLUF proteins
Seeing the light with BLUF proteins
复制标题
DOI：
10.1007/s12551-017-0258-6
复制
发表时间：
2017-03
影响因子：
--
通讯作者：
Sam-Yong Park;J. Tame
中科院分区：
文献类型：
--
作者：
Sam-Yong Park;J. Tame
BLUF （Blue Light Using Flavin）结构域在大约15年前首次被描述，它是一种光触发开关，控制酶活性或基因表达，以响应蓝光，在刺激后保持激活数秒甚至数分钟。这种保守的、类似铁氧化还原蛋白的折叠含有黄素发色团，它捕捉光并以某种方式触发下游事件。BLUF蛋白存在于原核生物和真核生物中，具有多种结构和寡聚形式，但BLUF结构域本身似乎具有保存完好的结构和机制，这是多年来研究的焦点。BLUF畴的晶体学和核磁共振结构已经得到了解决，但相互冲突的模型导致了对光活化的原子细节的大量争论。先进的光谱学和计算方法被用来分析光子吸收后的早期事件，但这些方法也导致了截然不同的结论。新的结构模型正在提高我们对机制细节的理解，并可能导致光遗传学的新型定制工具。
First described about 15 years ago, BLUF (Blue Light Using Flavin) domains are light-triggered switches that control enzyme activity or gene expression in response to blue light, remaining activated for seconds or even minutes after stimulation. The conserved, ferredoxin-like fold holds a flavin chromophore that captures the light and somehow triggers downstream events. BLUF proteins are found in both prokaryotes and eukaryotes and have a variety of architectures and oligomeric forms, but the BLUF domain itself seems to have a well-preserved structure and mechanism that have been the focus of intense study for a number of years. Crystallographic and NMR structures of BLUF domains have been solved, but the conflicting models have led to considerable debate about the atomic details of photo-activation. Advanced spectroscopic and computational methods have been used to analyse the early events after photon absorption, but these too have led to widely differing conclusions. New structural models are improving our understanding of the details of the mechanism and may lead to novel tailor-made tools for optogenetics.