6G7J

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 457-646 fs state structure

6G7J の概要

• エントリーDOI: 10.2210/pdb6g7j/pdb
• 分子名称: Bacteriorhodopsin, RETINAL, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, ... (5 entities in total)
• 機能のキーワード: retinal isomerization, ultrafast, femtosecond, room temperature, time resolved crystallography, photosynthesis
• 由来する生物種: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34454.59

構造登録者

Nogly, P.,Weinert, T.,James, D.,Cabajo, S.,Ozerov, D.,Furrer, A.,Gashi, D.,Borin, V.,Skopintsev, P.,Jaeger, K.,Nass, K.,Bath, P.,Bosman, R.,Koglin, J.,Seaberg, M.,Lane, T.,Kekilli, D.,Bruenle, S.,Tanaka, T.,Wu, W.,Milne, C.,White, T.,Barty, A.,Weierstall, U.,Panneels, V.,Nango, E.,Iwata, S.,Hunter, M.,Schapiro, I.,Schertler, G.,Neutze, R.,Standfuss, J. (登録日: 2018-04-06, 公開日: 2018-06-27, 最終更新日: 2024-10-23)

主引用文献

Nogly, P.,Weinert, T.,James, D.,Carbajo, S.,Ozerov, D.,Furrer, A.,Gashi, D.,Borin, V.,Skopintsev, P.,Jaeger, K.,Nass, K.,Bath, P.,Bosman, R.,Koglin, J.,Seaberg, M.,Lane, T.,Kekilli, D.,Brunle, S.,Tanaka, T.,Wu, W.,Milne, C.,White, T.,Barty, A.,Weierstall, U.,Panneels, V.,Nango, E.,Iwata, S.,Hunter, M.,Schapiro, I.,Schertler, G.,Neutze, R.,Standfuss, J.
Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser.
Science, 361:-, 2018

PubMed Abstract: Ultrafast isomerization of retinal is the primary step in photoresponsive biological functions including vision in humans and ion transport across bacterial membranes. We used an x-ray laser to study the subpicosecond structural dynamics of retinal isomerization in the light-driven proton pump bacteriorhodopsin. A series of structural snapshots with near-atomic spatial resolution and temporal resolution in the femtosecond regime show how the excited all-trans retinal samples conformational states within the protein binding pocket before passing through a twisted geometry and emerging in the 13-cis conformation. Our findings suggest ultrafast collective motions of aspartic acid residues and functional water molecules in the proximity of the retinal Schiff base as a key facet of this stereoselective and efficient photochemical reaction.

PubMed: 29903883
DOI: 10.1126/science.aat0094

実験手法

X-RAY DIFFRACTION (1.9 Å)