NMR-Based Conformational Ensembles Explain pH-Gated Opening and Closing of OmpG Channel

The outer membrane protein G (OmpG) is a monomeric 33 kDa 14-stranded β-barrel membrane protein functioning as a nonspecific porin for the uptake of oligosaccharides in Escherichia coli. Two different crystal structures of OmpG obtained at different values of pH suggest a pH-gated pore opening mecha...

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Veröffentlicht in:	Journal of the American Chemical Society 2013-10, Vol.135 (40), p.15101-15113
Hauptverfasser:	Zhuang, Tiandi, Chisholm, Christina, Chen, Min, Tamm, Lukas K
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - metabolism Disulfides - chemistry Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Hydrogen-Ion Concentration Ion Channel Gating Magnetic Resonance Spectroscopy Micelles Molecular Dynamics Simulation Mutagenesis, Site-Directed Mutation Phosphorylcholine - analogs & derivatives Phosphorylcholine - chemistry Porins - chemistry Porins - genetics Porins - metabolism Protein Conformation
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