6RQO

Steady-state-SMX activated state structure of bacteriorhodopsin

6RQO の概要

• エントリーDOI: 10.2210/pdb6rqo/pdb
• 関連するPDBエントリー: 6RNJ 6RPH
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: retinal, serial crystallography, time-resolved crystallography, tr-smx, proton transport
• 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: 24757.40

構造登録者

Weinert, T.,Skopintsev, P.,James, D.,Kekilli, D.,Furrer, A.,Bruenle, S.,Mous, S.,Nogly, P.,Standfuss, J. (登録日: 2019-05-16, 公開日: 2019-07-17, 最終更新日: 2024-01-24)

主引用文献

Weinert, T.,Skopintsev, P.,James, D.,Dworkowski, F.,Panepucci, E.,Kekilli, D.,Furrer, A.,Brunle, S.,Mous, S.,Ozerov, D.,Nogly, P.,Wang, M.,Standfuss, J.
Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography.
Science, 365:61-65, 2019

PubMed Abstract: Conformational dynamics are essential for proteins to function. We adapted time-resolved serial crystallography developed at x-ray lasers to visualize protein motions using synchrotrons. We recorded the structural changes in the light-driven proton-pump bacteriorhodopsin over 200 milliseconds in time. The snapshot from the first 5 milliseconds after photoactivation shows structural changes associated with proton release at a quality comparable to that of previous x-ray laser experiments. From 10 to 15 milliseconds onwards, we observe large additional structural rearrangements up to 9 angstroms on the cytoplasmic side. Rotation of leucine-93 and phenylalanine-219 opens a hydrophobic barrier, leading to the formation of a water chain connecting the intracellular aspartic acid-96 with the retinal Schiff base. The formation of this proton wire recharges the membrane pump with a proton for the next cycle.

PubMed: 31273117
DOI: 10.1126/science.aaw8634

実験手法

X-RAY DIFFRACTION (2 Å)