5VN9

Structure of bacteriorhodopsin from crystals grown at 4 deg C using GlyNCOC15+4 as an LCP host lipid

5VN9 の概要

• エントリーDOI: 10.2210/pdb5vn9/pdb
• 関連するPDBエントリー: 5VN7
• 分子名称: Bacteriorhodopsin (2 entities in total)
• 機能のキーワード: membrane protein, 7tm, retinal protein
• 由来する生物種: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
• 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: 57075.02

構造登録者

Ishchenko, A.,Peng, L.,Zinovev, E.,Vlasov, A.,Lee, S.C.,Kuklin, A.,Mishin, A.,Borshchevskiy, V.,Zhang, Q.,Cherezov, V. (登録日: 2017-04-28, 公開日: 2017-07-12, 最終更新日: 2023-10-04)

主引用文献

Ishchenko, A.,Peng, L.,Zinovev, E.,Vlasov, A.,Lee, S.C.,Kuklin, A.,Mishin, A.,Borshchevskiy, V.,Zhang, Q.,Cherezov, V.
Chemically Stable Lipids for Membrane Protein Crystallization.
Cryst Growth Des, 17:3502-3511, 2017

PubMed Abstract: Lipidic cubic phase (LCP) has been widely recognized as a promising membrane-mimicking matrix for biophysical studies of membrane proteins and their crystallization in a lipidic environment. Application of this material to a wide variety of membrane proteins, however, is hindered due to a limited number of available host lipids, mostly monoacylglycerols (MAGs). Here, we designed, synthesized and characterized a series of chemically stable lipids resistant to hydrolysis, with properties complementary to the widely used MAGs. In order to assess their potential to serve as host lipids for crystallization, we characterized the phase properties and lattice parameters of mesophases made of two most promising lipids at a variety of different conditions by polarized light microscopy and small-angle X-ray scattering. Both lipids showed remarkable chemical stability and an extended LCP region in the phase diagram covering a wide range of temperatures down to 4 °C. One of these lipids has been used for crystallization and structure determination of a prototypical membrane protein bacteriorhodopsin at 4 °C and 20 °C.

PubMed: 29290736
DOI: 10.1021/acs.cgd.7b00458

実験手法

X-RAY DIFFRACTION (2.594 Å)