Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
Nature Chemical Biology, ISSN: 1552-4469, Vol: 2, Issue: 11, Page: 627-635
2006
- 109Citations
- 95Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations109
- Citation Indexes109
- 109
- CrossRef104
- Captures95
- Readers95
- 95
Article Description
The molecular forces that drive structural transitions between the open and closed states of channels and transporters are not well understood. The gate of the OmpA channel is formed by the central Glu52-Arg138 salt bridge, which can open to form alternate ion pairs with Lys82 and Glu128. To gain deeper insight into the channel-opening mechanism, we measured interaction energies between the relevant side chains by double-mutant cycle analysis and correlated these with the channel activities of corresponding point mutants. The closed central salt bridge has a strong interaction energy of -5.6 kcal mol, which can be broken by forming the open-state salt bridge Glu52-Lys82 (ΔΔ G = -3.5 kcal mol) and a weak interaction between Arg138 and Glu128 (ΔΔG = -0.6 kcal mol ). A covalent disulfide bond in place of the central salt bridge completely blocks the channel. Growth assays indicate that this gating mechanism could physiologically contribute to the osmoprotection of Escherichia coli cells from environmental stress. © 2006 Nature Publishing Group.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33750255413&origin=inward; http://dx.doi.org/10.1038/nchembio827; http://www.ncbi.nlm.nih.gov/pubmed/17041590; https://www.nature.com/doifinder/10.1038/nchembio827; https://dx.doi.org/10.1038/nchembio827; https://www.nature.com/articles/nchembio827
Springer Science and Business Media LLC
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