Structural highlights
Function
[EXBB_ECO57] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). [EXBD_ECO57] Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates.
Publication Abstract from PubMed
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.
Structural insight into the role of the Ton complex in energy transduction.,Celia H, Noinaj N, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R, Buchanan SK Nature. 2016 Sep 21. doi: 10.1038/nature19757. PMID:27654919[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Celia H, Noinaj N, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R, Buchanan SK. Structural insight into the role of the Ton complex in energy transduction. Nature. 2016 Sep 21. doi: 10.1038/nature19757. PMID:27654919 doi:http://dx.doi.org/10.1038/nature19757
