Structural insight into the role of the Ton complex in energy transduction
Herve Celia,Nicholas Noinaj,Stanislav D. Zakharov,Enrica Bordignon,Istvan Botos,Monica Santamaria,Travis J. Barnard,William A. Cramer,Roland Lloubès,Susan K. Buchanan +9 more
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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.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.read more
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Structural basis for nutrient acquisition by dominant members of the human gut microbiota.
Amy J. Glenwright,Karunakar R. Pothula,Satya Prathyusha Bhamidimarri,Dror S. Chorev,Arnaud Baslé,Susan J. Firbank,Hongjun Zheng,Carol V. Robinson,Mathias Winterhalter,Ulrich Kleinekathöfer,David N. Bolam,Bert van den Berg +11 more
TL;DR: X-ray crystal structures of two functionally distinct SusCD complexes purified from Bacteroides thetaiotaomicron are presented and a general model for substrate translocation is derived to provide mechanistic insights into outer membrane nutrient import by members of the microbiota, an area of major importance for understanding human–microbiota symbiosis.
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Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry
Dror S. Chorev,Lindsay A Baker,Di Wu,Victoria Beilsten-Edmands,Sarah L. Rouse,Tzviya Zeev-Ben-Mordehai,Chimari Jiko,Firdaus Samsudin,Christoph Gerle,Syma Khalid,Alastair G. Stewart,Alastair G. Stewart,Stephen Matthews,Kay Grünewald,Kay Grünewald,Carol V. Robinson +15 more
TL;DR: In this article, the authors identified chaperone-porin association and lipid interactions in the β-barrel assembly machinery from Escherichia coli outer membranes, and from inner membranes they identified a pentameric pore of TonB, as well as the proteinconducting channel SecYEG in association with F 1 F O adenosine triphosphate (ATP) synthase.
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Structure and Function of Stator Units of the Bacterial Flagellar Motor
Mònica Santiveri,Aritz Roa-Eguiara,Caroline Kühne,Navish Wadhwa,Haidai Hu,Howard C. Berg,Marc Erhardt,Nicholas M.I. Taylor +7 more
TL;DR: This work identifies key residues involved in torque generation and presents a detailed mechanistic model for motor function and switching of rotational direction in the stator unit.
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Structures of the stator complex that drives rotation of the bacterial flagellum.
Justin C. Deme,Steven Johnson,Owen N. Vickery,Owen N. Vickery,Amy Aron,Holly Monkhouse,Thomas Griffiths,Rory Hennell James,Ben C. Berks,James W. Coulton,Phillip J. Stansfeld,Phillip J. Stansfeld,Susan M. Lea +12 more
TL;DR: Comparison to structures of other ion-driven motors indicates that this A 5 B 2 architecture is fundamental to bacterial systems that couple energy from ion flow to generate mechanical work at a distance and suggests that such events involve rotation in the motor structures.
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The contribution of modern EPR to structural biology.
TL;DR: Electron paramagnetic resonance (EPR) spectroscopy combined with site-directed spin labelling is applicable to biomolecules and their complexes irrespective of system size and in a broad range of environments.
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