5SV1

Structure of the ExbB/ExbD complex from E. coli at pH 4.5

Summary for 5SV1

• Entry DOI: 10.2210/pdb5sv1/pdb
• Related: 5SV0
• Descriptor: Biopolymer transport protein ExbB, Biopolymer transport protein ExbD, MERCURY (II) ION (3 entities in total)
• Functional Keywords: exbb, membrane proteins, pore, channel, transport protein
• Biological source: Escherichia coli DH1; More
• Total number of polymer chains: 12
• Total formula weight: 278240.47

Authors

Celia, H.,Botos, I.,Lloubes, R.,Buchanan, S.K.,Noinaj, N. (deposition date: 2016-08-04, release date: 2016-09-28, Last modification date: 2023-10-04)

Primary citation

Celia, H.,Noinaj, N.,Zakharov, S.D.,Bordignon, E.,Botos, I.,Santamaria, M.,Barnard, T.J.,Cramer, W.A.,Lloubes, R.,Buchanan, S.K.
Structural insight into the role of the Ton complex in energy transduction.
Nature, 538:60-65, 2016

PubMed 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.

PubMed: 27654919
DOI: 10.1038/nature19757

Experimental method

X-RAY DIFFRACTION (3.5 Å)