Cryo-electron microscopy for structure analyses of membrane proteins in the lipid bilayer. (August 2016)

• Record Type: Journal Article
• Authors: Abe, Kazuhiro; Fujiyoshi, Yoshinori
• Is Part Of: Current opinion in structural biology. Volume 39(2016)
• Page Start: 71
• Page End: 78
• Publication Date: 2016-08
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2016.06.001
• Languages: English
• ISSNs: 0959-440X

Abstract

Graphical abstract: Highlights: Electron crystallography analyzes membrane protein structures in the lipid bilayer. Waters are visualized in aquaporin channel pore in the membrane environment. Medium-resolution structure can be determined using imperfect 2D crystals. Single particle-like analysis in the membrane-embedded form is prerequisite. Abstract : Asymmetric distributions of materials, such as ions, solutes, chemicals, and information across the bio-membrane, which are generated by membrane proteins, are crucial hallmarks of all living organisms. Since the appropriate asymmetric distribution depends on the precise function of membrane proteins in the lipid bilayer, structural and functional analyses of the membrane-embedded forms of these proteins are crucial toward elucidating their mechanisms. In this review, we provide remarkable examples of structural analyses of membrane proteins in lipid bilayers based on electron crystallography of two-dimensional crystals. We also discuss the recent development of single-particle cryo-electron microscopy and propose a conceptual strategy for structural analysis of membrane proteins in the lipid bilayer.