Mechanism of absorption wavelength shifts in anion channelrhodopsin-1 mutants
Mechanism of absorption wavelength shifts in anion channelrhodopsin-1 mutants
复制标题
阴离子通道rhodopsin-1突变体吸收波长变化的机制
DOI：
10.1016/j.bbabio.2020.148349
复制
发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Ishikita Hiroshi
中科院分区：
文献类型：
--
作者：
Tsujimura Masaki;Noji Tomoyasu;Saito Keisuke;Kojima Keiichi;Sudo Yuki;Ishikita Hiroshi
使用量子力学/分子力学方法，我们展示了Guillardia θ阴离子通道视紫红质-1（GtACR 1）的蛋白质环境如何移动吸收波长的机制。GtACR 1突变体M105 A、C133 A和C237 A的计算吸收波长与实验测量的波长一致。在研究的192个突变结构中，Thr 101、Cys 133、Pro208和Cys 237处的突变可能增加吸收波长。特别地，T101 AGtACR 1在HEK 293 T细胞中表达。测得的吸收波长比野生型高10 nm，与计算波长一致。(i)从席夫碱部分去除极性残基，（ii）向β-紫罗兰酮环部分添加极性或酸性残基，和（iii）添加大体积残基以增加β-紫罗兰酮和席夫碱部分的平面性是增加吸收波长的基础。
Using a quantum mechanical/molecular mechanical approach, we show the mechanisms of how the protein environment ofGuillardia thetaanion channelrhodopsin-1 (GtACR1) can shift the absorption wavelength. The calculated absorption wavelengths forGtACR1 mutants, M105A, C133A, and C237A are in agreement with experimentally measured wavelengths. Among 192 mutant structures investigated, mutations at Thr101, Cys133, Pro208, and Cys237 are likely to increase the absorption wavelength. In particular, T101AGtACR1 was expressed in HEK293T cells. The measured absorption wavelength is 10 nm higher than that of wild type, consistent with the calculated wavelength. (i) Removal of a polar residue from the Schiff base moiety, (ii) addition of a polar or acidic residue to theβ-ionone ring moiety, and (iii) addition of a bulky residue to increase the planarity of theβ-ionone and Schiff base moieties are the basis of increasing the absorption wavelength.