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A three-dimensional movie of structural changes in bacteriorhodopsin

Journal article
Authors E. Nango
A. Royant
M. Kubo
T. Nakane
Cecilia Wickstrand
T. Kimura
T. Tanaka
K. Tono
C. Y. Song
R. Tanaka
T. Arima
A. Yamashita
J. Kobayashi
T. Hosaka
E. Mizohata
P. Nogly
M. Sugahara
D. Nam
T. Nomura
T. Shimamura
D. Im
T. Fujiwara
Y. Yamanaka
B. Jeon
T. Nishizawa
K. Oda
M. Fukuda
Rebecka Andersson
Petra Båth
Robert Dods
J. Davidsson
S. Matsuoka
S. Kawatake
M. Murata
O. Nureki
S. Owada
T. Kameshima
T. Hatsui
Y. Joti
G. Schertler
M. Yabashi
A. N. Bondar
J. Standfuss
Richard Neutze
S. Iwata
Published in Science
Volume 354
Issue 6319
Pages 1552-1557
ISSN 0036-8075
Publication year 2016
Published at Department of Chemistry and Molecular Biology
Pages 1552-1557
Language en
Links doi.org/10.1126/science.aah3497
Keywords x-ray-radiation, photoactive yellow protein, vectorial proton transport, l-intermediate, schiff-base, angstrom resolution, l-photointermediate, crystal-structure, water-molecules, m-state
Subject categories Organic Chemistry

Abstract

Bacteriorhodopsin (bR) is a light-driven proton pump and a model membrane transport protein. We used time-resolved serial femtosecond crystallography at an x-ray free electron laser to visualize conformational changes in bR from nanoseconds to milliseconds following photoactivation. An initially twisted retinal chromophore displaces a conserved tryptophan residue of transmembrane helix F on the cytoplasmic side of the protein while dislodging a key water molecule on the extracellular side. The resulting cascade of structural changes throughout the protein shows how motions are choreographed as bR transports protons uphill against a transmembrane concentration gradient.

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