English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F-1-ATP synthase

MPS-Authors
/persons/resource/persons14866

Böckmann,  R. A.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15155

Grubmueller,  H.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

External Ressource
Fulltext (public)

599683.pdf
(Publisher version), 2MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Böckmann, R. A., & Grubmueller, H. (2002). Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F-1-ATP synthase. Nature Structural Biology, 9(3), 198-202. Retrieved from http://www.nature.com/nsmb/journal/v9/n3/pdf/nsb760.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F430-9
Abstract
The mitochondrial membrane protein FoF1-ATP synthase synthesizes adenosine triphosphate (ATP), the universal currency of energy in the cell. This process involves mechanochemical energy transfer from rotating asymmetric gamma- 'stalk' to the three active sites of the F-1 unit, which drives the bound ATP out of the binding pocket. Here, the primary structural changes associated with this energy transfer in F-1- ATP synthase were studied with multi-nanosecond molecular dynamics simulations. By forced rotation of the gamma-stalk that mimics the effect of proton motive F-o-rotation during ATP synthesis, time-resolved atomic model for the structural changes in the F-1 part in terms of propagating conformational motions is obtained. For these, different time scales are found, which allows the separation of nanosecond from microsecond conformational motions. In the simulations, rotation of the gamma-stalk lowers the ATP affinity of the beta(TP) binding pocket and triggers fast, spontaneous closure of the empty beta(E) subunit. The simulations explain several mutation studies and the reduced hydrolysis rate of gamma- depleted F-1-ATPase.