OmpA: a pore or not a pore? Simulation and modeling studies.

Journal article

The bacterial outer membrane protein OmpA is composed of an N-terminal 171-residue beta-barrel domain (OmpA(171)) that spans the bilayer and a periplasmic, C-terminal domain of unknown structure. OmpA has been suggested to primarily serve a structural role, as no continuous pore through the center of the barrel can be discerned in the crystal structure of OmpA(171). However, several groups have recorded ionic conductances for bilayer-reconstituted OmpA(171). To resolve this apparent paradox w...

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Authors: Bond, P; Faraldo-Gómez, J; Sansom, MS

• Publication status: Published
• Journal: Biophysical journal
• Volume: 83
• Issue: 2
• Pages: 763-775
• Publication date: 2002-08-01
• DOI: 10.1016/s0006-3495(02)75207-7
• EISSN: 1542-0086
• ISSN: 0006-3495
• Language: English
• Keywords: Glutamic Acid; Protein Structure, Tertiary; Arginine; Protein Structure, Secondary; Hydrogen Bonding; Protein Conformation; Biophysical Phenomena; Monte Carlo Method; Time Factors; Bacterial Outer Membrane Proteins; Biophysics; Computer Simulation; Models, Molecular