6G7H

Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: resting state structure

Summary for 6G7H

• Entry DOI: 10.2210/pdb6g7h/pdb
• Descriptor: Bacteriorhodopsin, RETINAL, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, ... (5 entities in total)
• Functional Keywords: retinal isomerization, ultrafast, femtosecond, room temperature, time resolved crystallography, proton transport
• Biological source: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
• Total number of polymer chains: 1
• Total formula weight: 32998.92

Authors

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. (deposition date: 2018-04-06, release date: 2018-06-27, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)