Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin
Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin
复制标题
酪氨酸185对七次跨膜受体细菌视紫红质视网膜异构化平衡和质子释放通道的介导机制
DOI：
10.1016/j.bbabio.2016.08.002
复制
发表时间：
2016-11-01
影响因子：
4.3
通讯作者：
Zhao, Xin
中科院分区：
文献类型：
--
作者：
Ding, Xiaoyan;Wang, Honglei;Zhao, Xin
静电耦合导致蛋白质构象变化的直接演示具有挑战性，它需要探索与功能描述相关的局部、离散的电子细节和动态信息。在这里，作为一项解决这一挑战的新研究，报道了芳香族残基在影响膜受体在其自然膜环境中的功能构象变化中的作用。以前难以处理的离散电子细节已经通过特殊标记的受体的2D固体核磁共振获得，并得到了分子动力学模拟、突变分析和功能分析的支持，并与刚性原子晶体结构模型进行了比较。氢键和疏水相互作用被认为是直接机电耦合到受体内构象变化动力学的机制来源。(C)2016爱思唯尔B.V.保留所有权利。
Electrostatic coupling leading to conformational changes in proteins is challenging to demonstrate directly, it requires that both the local, discrete electronic details and dynamic information relevant to the functional descriptions are probed. Here, as a novel study to address this challenge, the roles of an aromatic residue in influencing the functional conformational changes of a membrane receptor in its natural membrane environment are reported. Previously intractable discrete electronic details have been obtained using 2D solid-state NMR of specifically labelled receptor, reinforced with molecular dynamic simulations, mutational analysis and functional assays, supported by and compared with rigid-atom crystal structural models. Hydrogen bonding and hydrophobic interactions are identified as the mechanistic origin for direct electromechanical coupling to the dynamics of conformational changes within the receptor. (C) 2016 Elsevier B.V. All rights reserved.