3HAN

Crystal structure of bacteriorhodopsin mutant V49A crystallized from bicelles

3HAN の概要

• エントリーDOI: 10.2210/pdb3han/pdb
• 関連するPDBエントリー: 3HAO 3HAP 3HAQ 3HAR 3HAS
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: bacteriorhodopsin, packing force, van der waals, evolutionary constraint, membrane protein, integral membrane protein, helical membrane protein, proton transport, cell membrane, chromophore, hydrogen ion transport, ion transport, membrane, photoreceptor protein, pyrrolidone carboxylic acid, receptor, retinal protein, sensory transduction, transmembrane, transport, transport protein
• 由来する生物種: Halobacterium salinarum (Halobacterium halobium)
• 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: 27185.88

構造登録者

Joh, N.H.,Yang, D.,Bowie, J.U. (登録日: 2009-05-02, 公開日: 2009-09-22, 最終更新日: 2024-11-06)

主引用文献

Joh, N.H.,Oberai, A.,Yang, D.,Whitelegge, J.P.,Bowie, J.U.
Similar energetic contributions of packing in the core of membrane and water-soluble proteins.
J.Am.Chem.Soc., 131:10846-10847, 2009

PubMed Abstract: A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins.

PubMed: 19603754
DOI: 10.1021/ja904711k

実験手法

X-RAY DIFFRACTION (2.75 Å)