6RMK

Bacteriorhodopsin, dark state, cell 2, refined using the same protocol as sub-ps time delays

6RMK の概要

• エントリーDOI: 10.2210/pdb6rmk/pdb
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: membrane protein, proton pump, time-resolved crystallography, free-electron laser
• 由来する生物種: Halobacterium salinarum NRC-1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25588.32

構造登録者

Nass Kovacs, G.,Colletier, J.-P.,Gruenbein, M.L.,Stensitzki, T.,Batyuk, A.,Carbajo, S.,Doak, R.B.,Ehrenberg, D.,Foucar, L.,Gasper, R.,Gorel, A.,Hilpert, M.,Kloos, M.,Koglin, J.,Reinstein, J.,Roome, C.M.,Schlesinger, R.,Seaberg, M.,Shoeman, R.L.,Stricker, M.,Boutet, S.,Haacke, S.,Heberle, J.,Domratcheva, T.,Barends, T.R.M.,Schlichting, I. (登録日: 2019-05-07, 公開日: 2019-06-05, 最終更新日: 2024-10-16)

主引用文献

Nass Kovacs, G.,Colletier, J.P.,Grunbein, M.L.,Yang, Y.,Stensitzki, T.,Batyuk, A.,Carbajo, S.,Doak, R.B.,Ehrenberg, D.,Foucar, L.,Gasper, R.,Gorel, A.,Hilpert, M.,Kloos, M.,Koglin, J.E.,Reinstein, J.,Roome, C.M.,Schlesinger, R.,Seaberg, M.,Shoeman, R.L.,Stricker, M.,Boutet, S.,Haacke, S.,Heberle, J.,Heyne, K.,Domratcheva, T.,Barends, T.R.M.,Schlichting, I.
Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin.
Nat Commun, 10:3177-3177, 2019

PubMed Abstract: Bacteriorhodopsin (bR) is a light-driven proton pump. The primary photochemical event upon light absorption is isomerization of the retinal chromophore. Here we used time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy were used to identify a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multiphoton effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.

PubMed: 31320619
DOI: 10.1038/s41467-019-10758-0

実験手法

X-RAY DIFFRACTION (1.8 Å)