English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Allegretti, M., Klusch, N., Mills, D. J., Vonck, J., Kühlbrandt, W., & Davies, K. M. (2015). Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase. Nature, 521, 237-240. doi:10.1038/nature14185.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Allegretti, Matteo1, Author              
Klusch, Niklas1, Author
Mills, Deryck J.1, Author
Vonck, Janet1, Author              
Kühlbrandt, Werner1, Author              
Davies, Karen M.1, Author              
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

Content

show
hide
Free keywords: Cryoelectron microscopy; Bioenergetics
 Abstract: -

Details

show
hide
Language(s): eng - English
 Dates: 20142014-08-282014-12-292015-02-232015-05-14
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: ATP, the universal energy currency of cells, is produced by F-type ATP synthases, which are ancient, membrane-bound nanomachines. F-type ATP synthases use the energy of a transmembrane electrochemical gradient to generate ATP by rotary catalysis. Protons moving across the membrane drive a rotor ring composed of 8–15 c-subunits. A central stalk transmits the rotation of the c-ring to the catalytic F1 head, where a series of conformational changes results in ATP synthesis. A key unresolved question in this fundamental process is how protons pass through the membrane to drive ATP production. Mitochondrial ATP synthases form V-shaped homodimers in cristae membranes. Here we report the structure of a native and active mitochondrial ATP synthase dimer, determined by single-particle electron cryomicroscopy at 6.2 Å resolution. Our structure shows four long, horizontal membrane-intrinsic α-helices in the a-subunit, arranged in two hairpins at an angle of approximately 70° relative to the c-ring helices. It has been proposed that a strictly conserved membrane-embedded arginine in the a-subunit couples proton translocation to c-ring rotation. A fit of the conserved carboxy-terminal a-subunit sequence places the conserved arginine next to a proton-binding c-subunit glutamate. The map shows a slanting solvent-accessible channel that extends from the mitochondrial matrix to the conserved arginine. Another hydrophilic cavity on the lumenal membrane surface defines a direct route for the protons to an essential histidine–glutamate pair. Our results provide unique new insights into the structure and function of rotary ATP synthases and explain how ATP production is coupled to proton translocation.
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/nature14185
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 521 Sequence Number: - Start / End Page: 237 - 240 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238