Conformational switching in the fungal light sensor vivid
Conformational switching in the fungal light sensor vivid
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DOI：
10.1126/science.1137128
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发表时间：
2007-05-18
期刊：
影响因子：
56.9
通讯作者：
Crane, Brian R.
中科院分区：
文献类型：
--
作者：
Zoltowski, Brian D.;Schwerdtfeger, Carsten;Crane, Brian R.
粗糙脉孢菌感光体Vivid调谐蓝光响应并调节生物钟的门控。晶体结构的暗态和亮态生动揭示了一个光，氧，或电压Per-Arnt-Sim域与一个不寻常的N-末端帽区和一个环插入，可容纳黄素辅因子。半胱氨酸-黄素加合物的光诱导形成驱动黄素质子化以诱导N-末端构象变化。远离黄素腺嘌呤二核苷酸结合位点的半胱氨酸到丝氨酸的取代使黄素光循环的构象转换变得复杂，并阻止Vivid在脉孢菌中发送信号。这种激活机制的关键元件由其他光传感器如白色Collar-1、ZEITLUPE、ENVOY和黄素结合、kelch重复序列、F-BOX 1（FKF 1）保存。
The Neurospora crassa photoreceptor Vivid tunes blue-light responses and modulates gating of the circadian clock. Crystal structures of dark-state and light-state Vivid reveal a light, oxygen, or voltage Per-Arnt-Sim domain with an unusual N-terminal cap region and a loop insertion that accommodates the flavin cofactor. Photoinduced formation of a cystein-flavin adduct drives flavin protonation to induce an N-terminal conformational change. A cysteine-to-serine substitution remote from the flavin adenine dinucleotide binding site decouples conformational switching from the flavin photocycle and prevents Vivid from sending signals in Neurospora. Key elements of this activation mechanism are conserved by other photosensors such as White Collar-1, ZEITLUPE, ENVOY, and flavin-binding, kelch repeat, F-BOX 1 ( FKF1).