1VJM

Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin

「1R3P」から置き換えられました

1VJM の概要

• エントリーDOI: 10.2210/pdb1vjm/pdb
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: ion transport, photoreceptor, transmembrane, retinal protein, hydrogen ion transport, transport protein
• 由来する生物種: Halobacterium sp.
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P02945
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27213.94

構造登録者

Edman, K.,Royant, A.,Larsson, G.,Jacobson, F.,Taylor, T.,van der Spoel, D.,Landau, E.M.,Pebay-Peyroula, E.,Neutze, R. (登録日: 2004-03-12, 公開日: 2004-04-06, 最終更新日: 2024-10-23)

主引用文献

Edman, K.,Royant, A.,Larsson, G.,Jacobson, F.,Taylor, T.,van der Spoel, D.,Landau, E.M.,Pebay-Peyroula, E.,Neutze, R.
Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsin.
J.Biol.Chem., 279:2147-2158, 2004

PubMed Abstract: X-ray and electron diffraction studies of specific reaction intermediates, or reaction intermediate analogues, have produced a consistent picture of the structural mechanism of light-driven proton pumping by bacteriorhodopsin. Of central importance within this picture is the structure of the L-intermediate, which follows the retinal all-trans to 13-cis photoisomerization step of the K-intermediate and sets the stage for the primary proton transfer event from the positively charged Schiff base to the negatively charged Asp-85. Here we report the structural changes in bacteriorhodopsin following red light illumination at 150 K. Single crystal microspectrophotometry showed that only the L-intermediate is populated in three-dimensional crystals under these conditions. The experimental difference Fourier electron density map and refined crystallographic structure were consistent with those previously presented (Royant, A., Edman, K., Ursby, T., Pebay-Peyroula, E., Landau, E. M., and Neutze, R. (2000) Nature 406, 645-648; Royant, A., Edman, K., Ursby, T., Pebay-Peyroula, E., Landau, E. M., and Neutze, R. (2001) Photochem. Photobiol. 74, 794-804). Based on the refined crystallographic structures, molecular dynamic simulations were used to examine the influence of the conformational change of the protein that is associated with the K-to-L transition on retinal dynamics. Implications regarding the structural mechanism for proton pumping by bacteriorhodopsin are discussed.

PubMed: 14532280
DOI: 10.1074/jbc.M300709200

実験手法

X-RAY DIFFRACTION (2.3 Å)