1C8R

BACTERIORHODOPSIN D96N BR STATE AT 2.0 A RESOLUTION

1C8R の概要

• エントリーDOI: 10.2210/pdb1c8r/pdb
• 関連するPDBエントリー: 1C3W 1C8S
• 分子名称: PROTEIN (BACTERIORHODOPSIN), 1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL, 2,10,23-TRIMETHYL-TETRACOSANE, ... (5 entities in total)
• 機能のキーワード: ion pump, membrane protein, retinal protein, lipids, photoreceptor, haloarchaea, d96n br state, ion transport, merohedral twinning, proton transport
• 由来する生物種: Halobacterium salinarum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35902.38

構造登録者

Luecke, H. (登録日: 1999-07-29, 公開日: 1999-10-20, 最終更新日: 2024-10-30)

主引用文献

Luecke, H.,Schobert, B.,Richter, H.T.,Cartailler, J.P.,Lanyi, J.K.
Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution.
Science, 286:255-260, 1999

PubMed Abstract: Crystal structures of the Asp96 to Asn mutant of the light-driven proton pump bacteriorhodopsin and its M photointermediate produced by illumination at ambient temperature have been determined to 1.8 and 2.0 angstroms resolution, respectively. The trapped photoproduct corresponds to the late M state in the transport cycle-that is, after proton transfer to Asp85 and release of a proton to the extracellular membrane surface, but before reprotonation of the deprotonated retinal Schiff base. Its density map describes displacements of side chains near the retinal induced by its photoisomerization to 13-cis,15-anti and an extensive rearrangement of the three-dimensional network of hydrogen-bonded residues and bound water that accounts for the changed pKa values (where Ka is the acid constant) of the Schiff base and Asp85. The structural changes detected suggest the means for conserving energy at the active site and for ensuring the directionality of proton translocation.

PubMed: 10514362
DOI: 10.1126/science.286.5438.255

実験手法

X-RAY DIFFRACTION (1.8 Å)