English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Engineering rotor ring stoichiometries in the ATP synthase

Pogoryelov, D., Klyszejko, A., Krasnoselska, G. O., Heller, E.-M., Leone, V., Langer, J. D., et al. (2012). Engineering rotor ring stoichiometries in the ATP synthase. Proceedings of the National Academy of Sciences of the United States of America, 109(25), E1599-E1608. doi:10.1073/pnas.1120027109.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Pogoryelov, Denys1, Author              
Klyszejko, Adriana1, 2, Author              
Krasnoselska, Ganna O.1, Author              
Heller, Eva-Maria1, Author              
Leone, Vanessa3, Author              
Langer, Julian David4, Author              
Vonck, Janet1, Author              
Müller, Daniel J.5, Author
Faraldo-Gómez, José D.3, 6, Author              
Meier, Thomas1, Author              
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Biotechnology Center, Dresden University of Technology, 01307 Dresden, ou_persistent22              
3Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068295              
4Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
5Department of Biosystems Science and Engineering, Swiss Federal Institute of Technology Zürich, 4058 Basel, Switzerland, ou_persistent22              
6Cluster of Excellence Macromolecular Complexes, Max-Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany, ou_persistent22              

Content

show
hide
Free keywords: alpha helix packing; F1Fo ATP synthase; membrane protein; rotary motor stoichiometry; bioenergetics
 Abstract: ATP synthase membrane rotors consist of a ring of c-subunits whose stoichiometry is constant for a given species but variable across different ones. We investigated the importance of c/c-subunit contacts by site-directed mutagenesis of a conserved stretch of glycines (GxGxGxGxG) in a bacterial c11 ring. Structural and biochemical studies show a direct, specific influence on the c-subunit stoichiometry, revealing c< 11, c12, c13, c14, and c> 14 rings. Molecular dynamics simulations rationalize this effect in terms of the energetics and geometry of the c-subunit interfaces. Quantitative data from a spectroscopic interaction study demonstrate that the complex assembly is independent of the c-ring size. Real-time ATP synthesis experiments in proteoliposomes show the mutant enzyme, harboring the larger c12 instead of c11, is functional at lower ion motive force. The high degree of compliance in the architecture of the ATP synthase rotor offers a rationale for the natural diversity of c-ring stoichiometries, which likely reflect adaptations to specific bioenergetic demands. These results provide the basis for bioengineering ATP synthases with customized ion-to-ATP ratios, by sequence modifications.

Details

show
hide
Language(s): eng - English
 Dates: 2011-12-062012-04-252012-05-24
 Publication Status: Published online
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1120027109
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 109 (25) Sequence Number: - Start / End Page: E1599 - E1608 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230