A three-dimensional movie of structural changes in bacteriorhodopsin

  title={A three-dimensional movie of structural changes in bacteriorhodopsin},
  author={Eriko Nango and Antoine Royant and Minoru Kubo and Takanori Nakane and Cecilia Wickstrand and Tetsunari Kimura and Tomoyuki Tanaka and Kensuke Tono and Changyong Song and Rie Tanaka and Toshi Arima and Ayumi Yamashita and Junya Kobayashi and Toshiaki Hosaka and Eiichi Mizohata and Przemyslaw Nogly and Michihiro Sugahara and Daewoong Nam and Takashi Nomura and Tatsuro Shimamura and Dohyun Im and Takaaki Fujiwara and Yasuaki Yamanaka and Byeonghyun Jeon and Tomohiro Nishizawa and Kazumasa Oda and Masahiro Fukuda and Rebecka Andersson and Petra B{\aa}th and Robert H. Dods and Jan. Davidsson and Shigeru Matsuoka and Satoshi Kawatake and Michio Murata and Osamu Nureki and Shigeki Owada and Takashi Kameshima and Takaki Hatsui and Yasumasa Joti and Gebhard F. X. Schertler and Makina Yabashi and Ana‐Nicoleta Bondar and J{\"o}rg Standfuss and Richard Neutze and So Iwata},
  pages={1552 - 1557}
Snapshots of bacteriorhodopsin Bacteriorhodopsin is a membrane protein that harvests the energy content from light to transport protons out of the cell against a transmembrane potential. Nango et al. used timeresolved serial femtosecond crystallography at an x-ray free electron laser to provide 13 structural snapshots of the conformational changes that occur in the nanoseconds to milliseconds after photoactivation. These changes begin at the active site, propagate toward the extracellular side… 

Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography

Time-resolved serial crystallography completes the dynamic view of proton pumping in a light-powered membrane protein with large conformational changes in the proton pump bacteriorhodopsin that allow for redistribution of protons during the pumping cycle.

Retinal isomerization in bacteriorhodopsin captured by a femtosecond x-ray laser

The principal mechanism of isomerization in this prototypical retinal-binding protein has direct relevance for all other members of this important family of membrane proteins, and it provides insight into how protein environments catalyze photochemical reactions in general.

Femtosecond-to-millisecond structural changes in a light-driven sodium pump

Crystallographic ‘snapshots’ taken at intervals of femtoseconds to milliseconds after activation show how a light-activated sodium pump carries sodium ions across the cell membrane and provide direct molecular insight into the dynamics of active cation transport across biological membranes.

Single molecule kinetics of bacteriorhodopsin by HS-AFM.

High-speed atomic force microscopy methods are used to characterize the single molecule kinetics of wild-type bR exposed to continuous light and short pulses, and determine that the cytoplasmic gate opens after photon absorption, and stays open for proton capture for 13.2 ms.

Dynamics of Bacteriorhodopsin in the Dark‐Adapted State from Solution Nuclear Magnetic Resonance Spectroscopy

A detailed picture of previously undescribed equilibrium dynamics on different time scales for ground-state bR is provided and is related to reorganization of the water network.

X-ray structure analysis of bacteriorhodopsin at 1.3 Å resolution

The accurate crystallographic analysis of bR in the ground state is reported, finding the twist of the retinal polyene was determined to be different from those in the previous models, and two conformations were observed for the proton release region.

O to bR transition in bacteriorhodopsin occurs through a proton hole mechanism

It is shown that the O to ground state transition in bR, in fact, features proton exchange between two distant groups via a proton hole mechanism, which provides an explanation for the observation that the D85S mutant of bacteriorhodopsin pumps chloride ions.

Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin

Time-resolved serial femtosecond crystallographic analyses of ChR are performed by using an X-ray free electron laser, which revealed conformational changes following photoactivation, which should be the triggers for opening of the ion conducting pore.

Hydroxide Ion Carrier for Proton Pump in Bacteriorhodopsin: Primary Proton Transfer

Bacteriorhodopsin (BR) is a model protein for light-driven proton pumps, where the vectorial active proton transport results in light-energy conversion. To clarify the microscopic mechanism of



High-resolution X-ray structure of an early intermediate in the bacteriorhodopsin photocycle

The high-resolution X-ray structure of an early intermediate in the photocycle of bacteriorhodopsin is described, which is formed directly after photoexcitation.

Molecular mechanism of vectorial proton translocation by bacteriorhodopsin

An atomic model for structural changes involved in the vectorial, light-driven transport of protons by bacteriorhodopsin is presented, which provides an ‘opening’ of the protein to protons on the cytoplasmic side of the membrane.

Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution.

X-ray diffraction of bacteriorhodopsin crystals grown in cubic lipid phase revealed unexpected two-fold symmetries that indicate merohedral twinning along the crystallographic c axis.

Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution.

Crystal structures of the Asp96 to Asn mutant of the light-driven proton pump bacteriorhodopsin and its M photointermediate produced by illumination at ambient temperature have been determined to 1.8

Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin

The structure of the late M intermediate of wild-type bacteriorhodopsin is determined and shows a water net that allows proton transfer from the proton donor group Asp 96 towards the Schiff base.

Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin.

The structural changes suggest that protonation of Asp85 initiates a cascade of atomic displacements in the extracellular region that cause release of a proton to the surface.