1R2N

NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin

1R2N の概要

• エントリーDOI: 10.2210/pdb1r2n/pdb
• 関連するPDBエントリー: 1BRR 1c3w 1qhj
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: proton pump, membrane protein, retinal protein, photoreceptor, haloarchaea, proton transport
• 由来する生物種: Halobacterium salinarium (archaea)
• 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

Patzelt, H.,Simon, B.,terLaak, A.,Kessler, B.,Kuhne, R.,Schmieder, P.,Oesterhaelt, D.,Oschkinat, H. (登録日: 2003-09-29, 公開日: 2003-10-28, 最終更新日: 2024-11-13)

主引用文献

Patzelt, H.,Simon, B.,terLaak, A.,Kessler, B.,Kuhne, R.,Schmieder, P.,Oesterhaelt, D.,Oschkinat, H.
The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy
Proc.Natl.Acad.Sci.USA, 99:9765-9770, 2002

PubMed Abstract: The two forms of bacteriorhodopsin present in the dark-adapted state, containing either all-trans or 13-cis,15-syn retinal, were examined by using solution state NMR, and their structures were determined. Comparison of the all-trans and the 13-cis,15-syn forms shows a shift in position of about 0.25 A within the pocket of the protein. Comparing this to the 13-cis,15-anti chromophore of the catalytic cycle M-intermediate structure, the 13-cis,15-syn form demonstrates a less pronounced up-tilt of the retinal C12[bond]C14 region, while leaving W182 and T178 essentially unchanged. The N[bond]H dipole of the Schiff base orients toward the extracellular side in both forms, however, it reorients toward the intracellular side in the 13-cis,15-anti configuration to form the catalytic M-intermediate. Thus, the change of the N[bond]H dipole is considered primarily responsible for energy storage, conformation changes of the protein, and the deprotonation of the Schiff base. The structural similarity of the all-trans and 13-cis,15-syn forms is taken as strong evidence for the ion dipole dragging model by which proton (hydroxide ion) translocation follows the change of the dipole.

PubMed: 12119389
DOI: 10.1073/pnas.132253899

実験手法

SOLUTION NMR