1FBK

CRYSTAL STRUCTURE OF CYTOPLASMICALLY OPEN CONFORMATION OF BACTERIORHODOPSIN

1FBK の概要

• エントリーDOI: 10.2210/pdb1fbk/pdb
• 関連するPDBエントリー: 1FBB
• 分子名称: BACTERIORHODOPSIN, RETINAL (2 entities in total)
• 機能のキーワード: proton pump, membrane protein, retinal protein, two-dimensional crystal electron diffraction, single crystal, 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: 26962.77

構造登録者

Subramaniam, S.,Henderson, R. (登録日: 2000-07-15, 公開日: 2000-08-09, 最終更新日: 2024-11-06)

主引用文献

Subramaniam, S.,Henderson, R.
Molecular mechanism of vectorial proton translocation by bacteriorhodopsin.
Nature, 406:653-657, 2000

PubMed Abstract: Bacteriorhodopsin, a membrane protein with a relative molecular mass of 27,000, is a light driven pump which transports protons across the cell membrane of the halophilic organism Halobacterium salinarum. The chromophore retinal is covalently attached to the protein via a protonated Schiff base. Upon illumination, retinal is isomerized. The Schiff base then releases a proton to the extracellular medium, and is subsequently reprotonated from the cytoplasm. An atomic model for bacteriorhodopsin was first determined by Henderson et al, and has been confirmed and extended by work in a number of laboratories in the last few years. Here we present an atomic model for structural changes involved in the vectorial, light-driven transport of protons by bacteriorhodopsin. A 'switch' mechanism ensures the vectorial nature of pumping. First, retinal unbends, triggered by loss of the Schiff base proton, and second, a protein conformational change occurs. This conformational change, which we have determined by electron crystallography at atomic (3.2 A in-plane and 3.6 A vertical) resolution, is largely localized to helices F and G, and provides an 'opening' of the protein to protons on the cytoplasmic side of the membrane.

PubMed: 10949309
DOI: 10.1038/35020614

実験手法

ELECTRON CRYSTALLOGRAPHY (3.2 Å)