4HWL

Crystal Structure Analysis of the Bacteriorhodopsin in Facial Amphiphile-7 DMPC Bicelle

Summary for 4HWL

• Entry DOI: 10.2210/pdb4hwl/pdb
• Descriptor: Bacteriorhodopsin, RETINAL, HEXANE, ... (6 entities in total)
• Functional Keywords: facial amphiphile-7 dmpc bicelle, alpha helical 7 transmembrane protein, photoreceptor, proton pump, retinal binding, transmembrane, proton transport
• Biological source: Halobacterium salinarum
• Cellular location: Cell membrane; Multi-pass membrane protein: P02945
• Total number of polymer chains: 2
• Total formula weight: 57846.44

Authors

Lee, S.,Stout, C.D.,Zhang, Q. (deposition date: 2012-11-08, release date: 2013-03-20, Last modification date: 2023-09-20)

Primary citation

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

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: 23479627
DOI: 10.1073/pnas.1221442110

Experimental method

X-RAY DIFFRACTION (2 Å)