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Journal Article

Projection structure of the monomeric porin OmpG at 6 å resolution

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Mills,  Deryck J.       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Vonck,  Janet       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Behlau, M., Mills, D. J., Quader, H., Kühlbrandt, W., & Vonck, J. (2001). Projection structure of the monomeric porin OmpG at 6 å resolution. Journal of Molecular Biology (London), 305(1), 71-77. doi:10.1006/jmbi.2000.4284.


Cite as: https://hdl.handle.net/21.11116/0000-0007-33A0-A
Abstract
The Escherichia coli porin OmpG, which acts as an efficient unspecific channel for mono-, di- and trisaccharides, has been purified and crystallized in two dimensions. Projection maps of two different crystal forms of OmpG at 6 Å resolution show that the protein has a β-barrel structure characteristic for outer membrane proteins, and that it does not form trimers, unlike most other porins such as OmpF and OmpC, but appears in monomeric form. The size of the barrel is ∼2.5 nm, indicating that OmpG may consist of 14 β-strands. The projection map suggests that the channel is restricted by internal loops.