4OV0

Structure of Bacteriorhdopsin Transferred from Amphipol A8-35 to a Lipidic Mesophase

4OV0 の概要

• エントリーDOI: 10.2210/pdb4ov0/pdb
• 分子名称: Bacteriorhodopsin, RETINAL (3 entities in total)
• 機能のキーワード: light-driven proton pump, retinal attached via schiff base, membrane, transport protein
• 由来する生物種: Halobacterium sp.
• 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: 27213.94

構造登録者

Polovinkin, V.,Gushchin, I.,Sintsov, M.,Round, E.,Balandin, T.,Chervakov, P.,Schevchenko, V.,Utrobin, P.,Popov, A.,Borshchevskiy, V.,Mishin, A.,Kuklin, A.,Willbold, D.,Popot, J.L.,Gordeliy, V. (登録日: 2014-02-19, 公開日: 2014-10-01, 最終更新日: 2024-11-27)

主引用文献

Polovinkin, V.,Gushchin, I.,Sintsov, M.,Round, E.,Balandin, T.,Chervakov, P.,Schevchenko, V.,Utrobin, P.,Popov, A.,Borshchevskiy, V.,Mishin, A.,Kuklin, A.,Willbold, D.,Chupin, V.,Popot, J.L.,Gordeliy, V.
High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase.
J.Membr.Biol., 247:997-1004, 2014

PubMed Abstract: Amphipols (APols) have become important tools for the stabilization, folding, and in vitro structural and functional studies of membrane proteins (MPs). Direct crystallization of MPs solubilized in APols would be of high importance for structural biology. However, despite considerable efforts, it is still not clear whether MP/APol complexes can form well-ordered crystals suitable for X-ray crystallography. In the present work, we show that an APol-trapped MP can be crystallized in meso. Bacteriorhodopsin (BR) trapped by APol A8-35 was mixed with a lipidic mesophase, and crystallization was induced by adding a precipitant. The crystals diffract beyond 2 Å. The structure of BR was solved to 2 Å and found to be indistinguishable from previous structures obtained after transfer from detergent solutions. We suggest the proposed protocol of in meso crystallization to be generally applicable to APol-trapped MPs.

PubMed: 25192977
DOI: 10.1007/s00232-014-9700-x

実験手法

X-RAY DIFFRACTION (2 Å)