7Q35

Crystal structure of the mutant bacteriorhodopsin pressurized with krypton

7Q35 の概要

• エントリーDOI: 10.2210/pdb7q35/pdb
• 分子名称: Bacteriorhodopsin, RETINAL, EICOSANE, ... (8 entities in total)
• 機能のキーワード: proton pump, membrane protein
• 由来する生物種: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36573.16

構造登録者

Melnikov, I.,Rulev, M.,Astashkin, R.,Kovalev, K.,Carpentier, P.,Gordeliy, V.,Popov, A. (登録日: 2021-10-27, 公開日: 2022-04-27, 最終更新日: 2024-10-23)

主引用文献

Melnikov, I.,Orekhov, P.,Rulev, M.,Kovalev, K.,Astashkin, R.,Bratanov, D.,Ryzhykau, Y.,Balandin, T.,Bukhdruker, S.,Okhrimenko, I.,Borshchevskiy, V.,Bourenkov, G.,Mueller-Dieckmann, C.,van der Linden, P.,Carpentier, P.,Leonard, G.,Gordeliy, V.,Popov, A.
High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action.
Commun Biol, 5:360-360, 2022

PubMed Abstract: In this work we examine how small hydrophobic molecules such as inert gases interact with membrane proteins (MPs) at a molecular level. High pressure atmospheres of argon and krypton were used to produce noble gas derivatives of crystals of three well studied MPs (two different proton pumps and a sodium light-driven ion pump). The structures obtained using X-ray crystallography showed that the vast majority of argon and krypton binding sites were located on the outer hydrophobic surface of the MPs - a surface usually accommodating hydrophobic chains of annular lipids (which are known structural and functional determinants for MPs). In conformity with these results, supplementary in silico molecular dynamics (MD) analysis predicted even greater numbers of argon and krypton binding positions on MP surface within the bilayer. These results indicate a potential importance of such interactions, particularly as related to the phenomenon of noble gas-induced anaesthesia.

PubMed: 35422073
DOI: 10.1038/s42003-022-03233-y

実験手法

X-RAY DIFFRACTION (2 Å)