1O0A

BACTERIORHODOPSIN L INTERMEDIATE AT 1.62 A RESOLUTION

1O0A の概要

• エントリーDOI: 10.2210/pdb1o0a/pdb
• 関連するPDBエントリー: 1C3W 1M0K 1M0L 1M0M
• 分子名称: Bacteriorhodopsin, RETINAL, 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, ... (5 entities in total)
• 機能のキーワード: ion pump, membrane protein, retinal protein, lipids, photoreceptor, haloarchaea, 7-transmembrane, serpentine, merohedral twinning, proton transport
• 由来する生物種: Halobacterium salinarum
• 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: 35903.36

構造登録者

Lanyi, J.K. (登録日: 2003-02-20, 公開日: 2003-04-22, 最終更新日: 2024-11-20)

主引用文献

Lanyi, J.K.,Schobert, B.
Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle.
J.Mol.Biol., 328:439-450, 2003

PubMed Abstract: We produced the L intermediate of the photocycle in a bacteriorhodopsin crystal in photo-stationary state at 170 K with red laser illumination at 60% occupancy, and determined its structure to 1.62 A resolution. With this model, high-resolution structural information is available for the initial bacteriorhodopsin, as well as the first five states in the transport cycle. These states involve photo-isomerization of the retinal and its initial configurational changes, deprotonation of the retinal Schiff base and the coupled release of a proton to the extracellular membrane surface, and the switch event that allows reprotonation of the Schiff base from the cytoplasmic side. The six structural models describe the transformations of the retinal and its interaction with water 402, Asp85, and Asp212 in atomic detail, as well as the displacements of functional residues farther from the Schiff base. The changes provide rationales for how relaxation of the distorted retinal causes movements of water and protein atoms that result in vectorial proton transfers to and from the Schiff base.

PubMed: 12691752
DOI: 10.1016/S0022-2836(03)00263-8

実験手法

X-RAY DIFFRACTION (1.62 Å)