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Structural insight into the role of the Ton complex in energy transduction.
- Source :
-
Nature [Nature] 2016 Oct 06; Vol. 538 (7623), pp. 60-65. Date of Electronic Publication: 2016 Sep 21. - Publication Year :
- 2016
-
Abstract
- In Gram-negative bacteria, outer membrane transporters import nutrients by coupling to an inner membrane protein complex called the Ton complex. The Ton complex consists of TonB, ExbB, and ExbD, and uses the proton motive force at the inner membrane to transduce energy to the outer membrane via TonB. Here, we structurally characterize the Ton complex from Escherichia coli using X-ray crystallography, electron microscopy, double electron-electron resonance (DEER) spectroscopy, and crosslinking. Our results reveal a stoichiometry consisting of a pentamer of ExbB, a dimer of ExbD, and at least one TonB. Electrophysiology studies show that the Ton subcomplex forms pH-sensitive cation-selective channels and provide insight into the mechanism by which it may harness the proton motive force to produce energy.<br />Competing Interests: The authors declare no competing financial interests.
- Subjects :
- Crystallography, X-Ray
Escherichia coli ultrastructure
Escherichia coli Proteins ultrastructure
Hydrogen-Ion Concentration
Membrane Proteins ultrastructure
Multiprotein Complexes ultrastructure
Escherichia coli chemistry
Escherichia coli Proteins chemistry
Escherichia coli Proteins metabolism
Membrane Proteins chemistry
Membrane Proteins metabolism
Multiprotein Complexes chemistry
Multiprotein Complexes metabolism
Proton-Motive Force
Subjects
Details
- Language :
- English
- ISSN :
- 1476-4687
- Volume :
- 538
- Issue :
- 7623
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 27654919
- Full Text :
- https://doi.org/10.1038/nature19757