title: Mediation mechanism of tyrosine 185 on the retinal isomerization equilibrium and the proton release channel in the seven-transmembrane receptor bacteriorhodopsin.
abstract: 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.
authors: Shanghai Key Laboratory of Magnetic Resonance, Department of Physics, East China Normal University, Shanghai 200062, PR China.
authors: Xiaoyan
authors: X
authors: Ding
authors: State Key Laboratory of Molecular Reaction Dynamics, Dalian, Institute of Chemical Physics, Chinese Academy of Sciences, Liaoning 116023, PR China.
authors: Honglei
authors: H
authors: Wang
authors: Shanghai Key Laboratory of Magnetic Resonance, Department of Physics, East China Normal University, Shanghai 200062, PR China.
authors: Bo
authors: B
authors: Peng
authors: Shanghai Key Laboratory of Magnetic Resonance, Department of Physics, East China Normal University, Shanghai 200062, PR China.
authors: Haolin
authors: H
authors: Cui
authors: Shanghai Key Laboratory of Magnetic Resonance, Department of Physics, East China Normal University, Shanghai 200062, PR China.
authors: Yujiao
authors: Y
authors: Gao
authors: The UK 850 MHz Solid-State NMR Facility, Department of Physics, University of Warwick, Coventry CV4 7AL, UK.
authors: Dinu
authors: D
authors: Iuga
authors: Biomembrane Structure Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors: Peter J
authors: PJ
authors: Judge
authors: State Key Laboratory of Molecular Reaction Dynamics, Dalian, Institute of Chemical Physics, Chinese Academy of Sciences, Liaoning 116023, PR China. Electronic address: ghli@dicp.ac.cn.
authors: Guohui
authors: G
authors: Li
authors: Biomembrane Structure Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: anthony.watts@bioch.ox.ac.uk.
authors: Anthony
authors: A
authors: Watts
authors: Shanghai Key Laboratory of Magnetic Resonance, Department of Physics, East China Normal University, Shanghai 200062, PR China. Electronic address: xzhao@phy.ecnu.edu.cn.
authors: Xin
authors: X
authors: Zhao
mesh_terms: D019943:Amino Acid Substitution; D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006217:Halobacterium / Q000737:chemistry; D007536:Isomerism; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D011522:Protons; D014443:Tyrosine / Q000737:chemistry / Q000235:genetics
chemical_list: D011522:Protons; D014443:Tyrosine; D001436:Bacteriorhodopsins
keywords: Aromatic residue; Electrostatic coupling; Functional conformational change; Mutational analysis and functional assays; Solid-state NMR