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Lipid binding attenuates channel closure of the outer membrane protein OmpF
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Liko, Idlir, Degiacomi, Matteo T., Lee, Sejeong, Newport, Thomas D., Gault, Joseph, Reading, Eamonn, Hopper, Jonathan T. S., Housden, Nicholas G., White, Paul, Colledge, Matthew, Sula, Altin, Wallace, B. A., Kleanthous, Colin, Stansfeld, Phillip J., Bayley, Hagan, Benesch, Justin L. P., Allison, Timothy M. and Robinson, Carol V. (2018) Lipid binding attenuates channel closure of the outer membrane protein OmpF. Proceedings of the National Academy of Sciences of the United States of America, 115 (26). pp. 6691-6696. doi:10.1073/pnas.1721152115
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Official URL: http://dx.doi.org/10.1073/pnas.1721152115
Abstract
Outer-membrane porins are often considered as passive conduits of small molecules across lipid bilayers. Using native mass spectrometry experiments we identify a pH-sensitive lipid-binding mechanism of outer membrane porin F, which enables increased threading of a colicin-derived peptide through open channels. Supported by molecular dynamics simulations and channel recording experiments, we posit that this mechanism attenuates channel opening in response to changes in environmental conditions, specifically pH. These findings have important consequences for mass spectrometry experiments, wherein the role of charge is often overlooked, and they also could help provide understanding of antibiotics that gain access to Gram-negative bacteria through porin-mediated pathways.
| Item Type: | Journal Article | ||||||
|---|---|---|---|---|---|---|---|
| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||
| Journal or Publication Title: | Proceedings of the National Academy of Sciences of the United States of America | ||||||
| Publisher: | National Academy of Sciences | ||||||
| ISSN: | 0027-8424 | ||||||
| Official Date: | 11 June 2018 | ||||||
| Dates: |
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| Volume: | 115 | ||||||
| Number: | 26 | ||||||
| Page Range: | pp. 6691-6696 | ||||||
| DOI: | 10.1073/pnas.1721152115 | ||||||
| Status: | Peer Reviewed | ||||||
| Publication Status: | Published | ||||||
| Access rights to Published version: | Open Access |
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