English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  A c Subunit with Four Transmembrane Helices and One Ion (Na+)-binding Site in an Archaeal ATP Synthase

Mayer, F., Leone, V., Langer, J. D., Faraldo-Gómez, J. D., & Müller, V. (2012). A c Subunit with Four Transmembrane Helices and One Ion (Na+)-binding Site in an Archaeal ATP Synthase. The Journal of Biological Chemistry, 287(47), 39327-39337.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-D540-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-D541-5
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Mayer, Florian, Author
Leone, Vanessa1, Author              
Langer, Julian D.2, Author
Faraldo-Gómez, Jóse D.1, Author              
Müller, Volker, Author
Affiliations:
1Max Planck Research Group of Theoretical Molecular Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068295              
2Max Planck Society, ou_persistent13              

Content

show
hide
Free keywords: -
 Abstract: The ion-driven membrane rotors of ATP synthases consist of multiple copies of subunit c, forming a closed ring. Subunit c typically comprises two transmembrane helices, and the c ring features an ion-binding site in between each pair of adjacent subunits. Here, we use experimental and computational methods to study the structure and specificity of an archaeal c subunit more akin to those of V-type ATPases, namely that from Pyrococcus furiosus. The c subunit was purified by chloroform/methanol extraction and determined to be 15.8 kDa with four predicted transmembrane helices. However, labeling withDCCDas well as Na+-DCCD competition experiments revealed only one binding site for DCCD and Na+, indicating that the mature c subunit of this A1AO ATP synthase is indeed of the V-type. A structural model generated computationally revealed one Na+-binding site within each of the c subunits, mediated by a conserved glutamate side chain alongside other coordinating groups. An intriguing second glutamate located in-between adjacent c subunits was ruled out as a functional Na+-binding site. Molecular dynamics simulations indicate that the c ring of P. furiosus is highly Na+-specific under in vivo conditions, comparable with the Na+-dependent V1VO ATPase from Enterococcus hirae. Interestingly, the same holds true for the c ring from the methanogenic archaeon Methanobrevibacter ruminantium, whose c subunits also feature a V-type architecture but carry two Na+-binding sites instead. These findings are discussed in light of their physiological relevance and with respect to the mode of ion coupling in A1AO ATP synthases.

Details

show
hide
Language(s): eng - English
 Dates: 2012-11-16
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 631483
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 287 (47) Sequence Number: - Start / End Page: 39327 - 39337 Identifier: -