1PY6

Bacteriorhodopsin crystallized from bicells

1PY6 の概要

• エントリーDOI: 10.2210/pdb1py6/pdb
• 関連するPDBエントリー: 1PXR 1PXS
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: membrane protein
• 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: 2
• 化学式量合計: 54427.87

構造登録者

Faham, S.,Yang, D.,Bare, E.,Yohannan, S.,Whitelegge, J.P.,Bowie, J.U. (登録日: 2003-07-08, 公開日: 2003-12-16, 最終更新日: 2024-10-30)

主引用文献

Faham, S.,Yang, D.,Bare, E.,Yohannan, S.,Whitelegge, J.P.,Bowie, J.U.
Side-chain Contributions to Membrane Protein Structure and Stability.
J.Mol.Biol., 335:297-305, 2004

PubMed Abstract: The molecular forces that stabilize membrane protein structure are poorly understood. To investigate these forces we introduced alanine substitutions at 24 positions in the B helix of bacteriorhodopsin and examined their effects on structure and stability. Although most of the results can be rationalized in terms of the folded structure, there are a number of surprises. (1) We find a remarkably high frequency of stabilizing mutations (17%), indicating that membrane proteins are not highly optimized for stability. (2) Helix B is kinked, with the kink centered around Pro50. The P50A mutation has no effect on stability, however, and a crystal structure reveals that the helix remains bent, indicating that tertiary contacts dominate in the distortion of this helix. (3) We find that the protein is stabilized by about 1kcal/mol for every 38A(2) of surface area buried, which is quite similar to soluble proteins in spite of their dramatically different environments. (4) We find little energetic difference, on average, in the burial of apolar surface or polar surface area, implying that van der Waals packing is the dominant force that drives membrane protein folding.

PubMed: 14659758
DOI: 10.1016/j.jmb.2003.10.041

実験手法

X-RAY DIFFRACTION (1.8 Å)