1C3W

BACTERIORHODOPSIN/LIPID COMPLEX AT 1.55 A RESOLUTION

1C3W の概要

• エントリーDOI: 10.2210/pdb1c3w/pdb
• 関連するPDBエントリー: 1BRX
• 分子名称: BACTERIORHODOPSIN (GROUND STATE WILD TYPE "BR"), 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, 7-transmembrane, serpentine, ion transport, merohedral twinning
• 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: 33317.73

構造登録者

Luecke, H. (登録日: 1999-07-28, 公開日: 1999-09-15, 最終更新日: 2024-10-16)

主引用文献

Luecke, H.,Schobert, B.,Richter, H.T.,Cartailler, J.P.,Lanyi, J.K.
Structure of bacteriorhodopsin at 1.55 A resolution.
J.Mol.Biol., 291:899-911, 1999

PubMed Abstract: Th?e atomic structure of the light-driven ion pump bacteriorhodopsin and the surrounding lipid matrix was determined by X-ray diffraction of crystals grown in cubic lipid phase. In the extracellular region, an extensive three-dimensional hydrogen-bonded network of protein residues and seven water molecules leads from the buried retinal Schiff base and the proton acceptor Asp85 to the membrane surface. Near Lys216 where the retinal binds, transmembrane helix G contains a pi-bulge that causes a non-proline? kink. The bulge is stabilized by hydrogen-bonding of the main-chain carbonyl groups of Ala215 and Lys216 with two buried water molecules located between the Schiff base and the proton donor Asp96 in the cytoplasmic region. The results indicate extensive involvement of bound water molecules in both the structure and the function of this seven-helical membrane protein. A bilayer of 18 tightly bound lipid chains forms an annulus around the protein in the crystal. Contacts between the trimers in the membrane plane are mediated almost exclusively by lipids.

PubMed: 10452895
DOI: 10.1006/jmbi.1999.3027

実験手法

X-RAY DIFFRACTION (1.55 Å)