1QKO

HIGH RESOLUTION X-RAY STRUCTURE OF AN EARLY INTERMEDIATE IN THE BACTERIORHODOPSIN PHOTOCYCLE

1QKO の概要

• エントリーDOI: 10.2210/pdb1qko/pdb
• 関連するPDBエントリー: 1AP9 1AT9 1BAC 1BAD 1BCT 1BHA 1BHB 1BRD 1BRR 1BRX 1QHJ 1QKP 2BRD
• 分子名称: BACTERIORHODOPSIN, RETINAL (3 entities in total)
• 機能のキーワード: photoreceptor, proton pump, membrane protein, retinal protein, intermediate state, photocycle, lipidic cubic phases
• 由来する生物種: HALOBACTERIUM SALINARIUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27098.85

構造登録者

Edman, K.,Nollert, P.,Royant, A.,Belrhali, H.,Pebay-Peyroula, E.,Hajdu, J.,Neutze, R.,Landau, E.M. (登録日: 1999-07-30, 公開日: 1999-10-24, 最終更新日: 2024-11-13)

主引用文献

Edman, K.,Nollert, P.,Royant, A.,Belrhali, H.,Pebay-Peyroula, E.,Hajdu, J.,Neutze, R.,Landau, E.M.
High Resolution X-Ray Structure of an Early Intermediate in the Bacteriorhodopsin Photocycle
Nature, 401:822-, 1999

PubMed Abstract: Bacteriorhodopsin is the simplest known photon-driven proton pump and as such provides a model for the study of a basic function in bioenergetics. Its seven transmembrane helices encompass a proton translocation pathway containing the chromophore, a retinal molecule covalently bound to lysine 216 through a protonated Schiff base, and a series of proton donors and acceptors. Photoisomerization of the all-trans retinal to the 13-cis configuration initiates the vectorial translocation of a proton from the Schiff base, the primary proton donor, to the extracellular side, followed by reprotonation of the Schiff base from the cytoplasm. Here we describe the high-resolution X-ray structure of an early intermediate in the photocycle of bacteriorhodopsin, which is formed directly after photoexcitation. A key water molecule is dislocated, allowing the primary proton acceptor, Asp 85, to move. Movement of the main-chain Lys 216 locally disrupts the hydrogen-bonding network of helix G, facilitating structural changes later in the photocycle.

PubMed: 10548112
DOI: 10.1038/44623

実験手法

X-RAY DIFFRACTION (2.1 Å)