Spontaneous formation of detergent micelles around the outer membrane protein OmpX

被引:42
作者
Böckmann, RA [1 ]
Caflisch, A [1 ]
机构
[1] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland
关键词
D O I
10.1529/biophysj.105.060426
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The structure and flexibility of the outer membrane protein X (OmpX) in a water-detergent solution and in pure water are investigated by molecular dynamics simulations on the 100-ns timescale and compared with NMR data. The simulations allow for an unbiased determination of the structure of detergent micelles and the protein-detergent mixed micelle. The short-chain lipid dihexanoylphosphatidylcholine, as a detergent, aggregates into pure micelles of similar to 18 molecules, or alternatively, it binds to the protein surface. The detergent binds in the form of a monolayer ring around the hydrophobic beta-barrel of OmpX rather than in a micellar-like oblate; similar to 40 dihexanoylphosphatidylcholine lipids are sufficient for an effective suppression of water from the surface of the beta-barrel region. The phospholipids bind also on the extracellular, protruding beta-sheet. Here, polar interactions between charged amino acids and phosphatidylcholine headgroups act as condensation seed for detergent micelle formation. The polar protein surface remains accessible to water molecules. In total, similar to 90-100 detergent molecules associate within the protein-detergent mixed micelle, in agreement with experimental estimates. The simulation results indicate that OmpX is not a water pore and support the proposed role of the protruding beta-sheet as a "fishing rod''.
引用
收藏
页码:3191 / 3204
页数:14
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