5VN9

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

Summary for 5VN9

• Entry DOI: 10.2210/pdb5vn9/pdb
• Related: 5VN7
• Descriptor: Bacteriorhodopsin (2 entities in total)
• Functional Keywords: membrane protein, 7tm, retinal protein
• Biological source: Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
• Cellular location: Cell membrane ; Multi-pass membrane protein : P02945
• Total number of polymer chains: 2
• Total formula weight: 57075.02

Authors

Ishchenko, A.,Peng, L.,Zinovev, E.,Vlasov, A.,Lee, S.C.,Kuklin, A.,Mishin, A.,Borshchevskiy, V.,Zhang, Q.,Cherezov, V. (deposition date: 2017-04-28, release date: 2017-07-12, Last modification date: 2023-10-04)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.594 Å)