English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Complete Ion-Coordination Structure in the Rotor Ring of Na+-Dependent F-ATP Synthases

Meier, T., Krah, A., Bond, P. J., Pogoryelov, D., Diederichs, K., & Faraldo-Gómez, J. D. (2009). Complete Ion-Coordination Structure in the Rotor Ring of Na+-Dependent F-ATP Synthases. Journal of Molecular Biology, 391(2), 498-507. doi:10.1016/j.jmb.2009.05.082.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Meier, Thomas1, 2, Author           
Krah, Alexander3, Author           
Bond, Peter J.3, Author           
Pogoryelov, Denys1, Author           
Diederichs, Kay4, Author
Faraldo-Gómez, José D.2, 3, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Cluster of Excellence Macromolecular Complexes, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany, ou_persistent22              
3Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068295              
4Department of Biology, University of Konstanz, 78457 Konstanz, Germany, ou_persistent22              

Content

show
hide
Free keywords: F1Fo-ATP synthase rotor; c-ring structure; ion coordination and selectivity; sodium-motive force; Ilyobacter tartaricus
 Abstract: The membrane-embedded rotors of Na+-dependent F-ATP synthases comprise 11 c-subunits that form a ring, with 11 Na+ binding sites in between adjacent subunits. Following an updated crystallographic analysis of the c-ring from Ilyobacter tartaricus, we report the complete ion-coordination structure of the Na+ sites. In addition to the four residues previously identified, there exists a fifth ligand, namely, a buried structural water molecule. This water is itself coordinated by Thr67, which, sequence analysis reveals, is the only residue involved in binding that distinguishes Na+ synthases from H+-ATP synthases known to date. Molecular dynamics simulations and free-energy calculations of the c-ring in a lipid membrane lend clear support to the notion that this fifth ligand is a water molecule, and illustrate its influence on the selectivity of the binding sites. Given the evolutionary ascendancy of sodium over proton bioenergetics, this structure uncovers an ancient strategy for selective ion coupling in ATP synthases.

Details

show
hide
Language(s): eng - English
 Dates: 2009-05-282009-05-042009-05-292009-06-032009-08-14
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jmb.2009.05.082
PMID: 19500592
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology
  Other : JMB
  Abbreviation : J. Mol. Biol.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Elsevier
Pages: - Volume / Issue: 391 (2) Sequence Number: - Start / End Page: 498 - 507 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/0022-2836