5ITE

2.2-Angstrom in meso crystal structure of Haloquadratum Walsbyi Bacteriorhodopsin (HwBR) from Octylglucoside (OG) Detergent Micelles

5ITE の概要

• エントリーDOI: 10.2210/pdb5ite/pdb
• 関連するPDBエントリー: 5ITC
• 分子名称: Bacteriorhodopsin-I, RETINAL, (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (5 entities in total)
• 機能のキーワード: bacteriorhodopsin from haloquadratum walsbyi, lipidic cubic phase (lcp), og detergent micelle, traditional, membrane protein
• 由来する生物種: Haloquadratum walsbyi
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q18DH8
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 91364.60

構造登録者

Broecker, J.,Eger, B.T.,Ernst, O.P. (登録日: 2016-03-16, 公開日: 2017-01-25, 最終更新日: 2024-11-06)

主引用文献

Broecker, J.,Eger, B.T.,Ernst, O.P.
Crystallogenesis of Membrane Proteins Mediated by Polymer-Bounded Lipid Nanodiscs.
Structure, 25:384-392, 2017

PubMed Abstract: For some membrane proteins, detergent-mediated solubilization compromises protein stability and functionality, often impairing biophysical and structural analyses. Hence, membrane-protein structure determination is a continuing bottleneck in the field of protein crystallography. Here, as an alternative to approaches mediated by conventional detergents, we report the crystallogenesis of a recombinantly produced membrane protein that never left a lipid bilayer environment. We used styrene-maleic acid (SMA) copolymers to solubilize lipid-embedded proteins into SMA nanodiscs, purified these discs by affinity and size-exclusion chromatography, and transferred proteins into the lipidic cubic phase (LCP) for in meso crystallization. The 2.0-Å structure of an α-helical seven-transmembrane microbial rhodopsin thus obtained is of high quality and virtually identical to the 2.2-Å structure obtained from traditional detergent-based purification and subsequent LCP crystallization.

PubMed: 28089451
DOI: 10.1016/j.str.2016.12.004

実験手法

X-RAY DIFFRACTION (2.182 Å)