1AP9

X-RAY STRUCTURE OF BACTERIORHODOPSIN FROM MICROCRYSTALS GROWN IN LIPIDIC CUBIC PHASES

1AP9 の概要

• エントリーDOI: 10.2210/pdb1ap9/pdb
• 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, microcrystals, microfocus beam, lipidic cubic phases
• 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: 27098.85

構造登録者

Pebay-Peyroula, E.,Rummel, G.,Rosenbusch, J.P.,Landau, E.M. (登録日: 1997-07-26, 公開日: 1998-09-16, 最終更新日: 2024-11-13)

主引用文献

Pebay-Peyroula, E.,Rummel, G.,Rosenbusch, J.P.,Landau, E.M.
X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases.
Science, 277:1676-1681, 1997

PubMed Abstract: Lipidic cubic phases provide a continuous three-dimensional bilayer matrix that facilitates nucleation and growth of bacteriorhodopsin microcrystals. The crystals diffract x-rays isotropically to 2.0 angstroms. The structure of this light-driven proton pump was solved at a resolution of 2.5 angstroms by molecular replacement, using previous results from electron crystallographic studies as a model. The earlier structure was generally confirmed, but several differences were found, including loop conformations and side chain residues. Eight water molecules are now identified experimentally in the proton pathway. These findings reveal the constituents of the proton translocation pathway in the ground state.

PubMed: 9287223
DOI: 10.1126/science.277.5332.1676

実験手法

X-RAY DIFFRACTION (2.35 Å)