4HWL
Crystal Structure Analysis of the Bacteriorhodopsin in Facial Amphiphile-7 DMPC Bicelle
4HWL の概要
エントリーDOI | 10.2210/pdb4hwl/pdb |
分子名称 | Bacteriorhodopsin, RETINAL, HEXANE, ... (6 entities in total) |
機能のキーワード | facial amphiphile-7 dmpc bicelle, alpha helical 7 transmembrane protein, photoreceptor, proton pump, retinal binding, transmembrane, proton transport |
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 | 57846.44 |
構造登録者 | |
主引用文献 | Lee, S.C.,Bennett, B.C.,Hong, W.X.,Fu, Y.,Baker, K.A.,Marcoux, J.,Robinson, C.V.,Ward, A.B.,Halpert, J.R.,Stevens, R.C.,Stout, C.D.,Yeager, M.J.,Zhang, Q. Steroid-based facial amphiphiles for stabilization and crystallization of membrane proteins. Proc.Natl.Acad.Sci.USA, 110:E1203-E1211, 2013 Cited by PubMed Abstract: Amphiphile selection is a critical step for structural studies of membrane proteins (MPs). We have developed a family of steroid-based facial amphiphiles (FAs) that are structurally distinct from conventional detergents and previously developed FAs. The unique FAs stabilize MPs and form relatively small protein-detergent complexes (PDCs), a property considered favorable for MP crystallization. We attempted to crystallize several MPs belonging to different protein families, including the human gap junction channel protein connexin 26, the ATP binding cassette transporter MsbA, the seven-transmembrane G protein-coupled receptor-like bacteriorhodopsin, and cytochrome P450s (peripheral MPs). Using FAs alone or mixed with other detergents or lipids, we obtained 3D crystals of the above proteins suitable for X-ray crystallographic analysis. The fact that FAs enhance MP crystallizability compared with traditional detergents can be attributed to several properties, including increased protein stability, formation of small PDCs, decreased PDC surface flexibility, and potential to mediate crystal lattice contacts. PubMed: 23479627DOI: 10.1073/pnas.1221442110 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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