Journal
PROTEIN SCIENCE
Volume 19, Issue 4, Pages 625-630Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.345
Keywords
TonB; outer membrane; active transport; EPR; DEER; polyproline II
Categories
Funding
- Deutsche Forschungsgemeinschaft [743/2-1]
- Natural Sciences and Engineering Research Council of Canada
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TonB from Escherichia coli and its homologues are critical for the uptake of siderophores through the outer membrane of Gram-negative bacteria using chemiosmotic energy. When different models for the mechanism of TonB mediated energy transfer from the inner to the outer membrane are discussed, one of the key questions is whether TonB spans the periplasm. In this article, we use long range distance measurements by spin-label pulsed EPR (Double Electron-Electron Resonance, DEER) and CD spectroscopy to show that the proline-rich segment of TonB exists in a PPII-like conformation. The result implies that the proline-rich segment of TonB possesses a length of more than 15 nm, sufficient to span the periplasm of Gram-negative bacteria.
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