English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase

Matthies, D., Zhou, W., Klyszejko, A. L., Anselmi, C., Yildiz, Ö., Brandt, K., et al. (2014). High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase. Nature Communications, 5: 5286. doi:10.1038/ncomms6286.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Matthies, Doreen1, Author           
Zhou, Wenchang2, Author
Klyszejko, Adriana L.1, Author
Anselmi, Claudio2, Author
Yildiz, Özkan1, Author           
Brandt, Karsten3, Author
Müller, Volker3, Author
Faraldo-Gómez, José D.2, Author
Faraldo-Gómez, José D.4, Author
Meier, Thomas1, 4, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Theoretical Molecular Biophysics Section, National Heart, Lung and Blood Institute, National Institutes of Health, Building 5635FL, Suite T-800, Bethesda, Maryland 20892, USA, ou_persistent22              
3Department of Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt am Main, Max-von-Laue-Str. 9, 60438 Frankfurt am Main, Germany, ou_persistent22              
4Cluster of Excellence Macromolecular Complexes, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: All rotary ATPases catalyse the interconversion of ATP and ADP-Pi through a mechanism that is coupled to the transmembrane flow of H(+) or Na(+). Physiologically, however, F/A-type enzymes specialize in ATP synthesis driven by downhill ion diffusion, while eukaryotic V-type ATPases function as ion pumps. To begin to rationalize the molecular basis for this functional differentiation, we solved the crystal structure of the Na(+)-driven membrane rotor of the Acetobacterium woodii ATP synthase, at 2.1 Å resolution. Unlike known structures, this rotor ring is a 9:1 heteromer of F- and V-type c-subunits and therefore features a hybrid configuration of ion-binding sites along its circumference. Molecular and kinetic simulations are used to dissect the mechanisms of Na(+) recognition and rotation of this c-ring, and to explain the functional implications of the V-type c-subunit. These structural and mechanistic insights indicate an evolutionary path between synthases and pumps involving adaptations in the rotor ring.

Details

show
hide
Language(s): eng - English
 Dates: 2014-11-102014
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/ncomms6286
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: 14 Volume / Issue: 5 Sequence Number: 5286 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723