English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Bayesian inference of rotor ring stoichiometry from electron microscopy images of archaeal ATP synthase

MPS-Authors
/persons/resource/persons145578

Cossio,  Pilar
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Biophysics of Tropical Diseases, Max Planck Tandem Group, University of Antioquia, Medellín, Colombia;

/persons/resource/persons137581

Allegretti,  Matteo
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137933

Vonck,  Janet
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons15259

Hummer,  Gerhard
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Department of Physics, Goethe University Frankfurt;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Cossio, P., Allegretti, M., Mayer, F., Müller, V., Vonck, J., & Hummer, G. (2018). Bayesian inference of rotor ring stoichiometry from electron microscopy images of archaeal ATP synthase. Microscopy, 67(5), 266-273. doi:10.1093/jmicro/dfy033.


Cite as: http://hdl.handle.net/21.11116/0000-0002-8050-2
Abstract
The ‘Bayesian inference of electron microscopy’ (BioEM) framework makes it possible to determine the stoichiometry of protein complexes using 3D coarse-grained models and a relatively small number of cryo-electron microscopy images as input. We applied the method to determine the most probable rotor ring stoichiometry of the archaeal Na+ ATP synthase from Pyrococcus furiosus, a multisubunit complex able to produce ATP under extreme conditions. Archaeal ATP synthases consist of a catalytic A1 part and a membrane-embedded AO portion. The AO portion is composed of a rotor ring and the a-subunit. The rotor ring of P. furiosus ATP synthase is composed of 16-kDa c-subunits, each consisting of four helices forming a bundle, with only one Na+-binding site per bundle. This ring was proposed to be decameric from LILBID-MS analysis of the entire ATP synthase. By contrast, the BioEM posterior favors a c9 ring stoichiometry. With BioEM, we ranked coarse-grained models of the whole complex with different ring geometry, using 6400 unprocessed particle images of the A1AO complex collected in vitreous ice. BioEM makes it possible to probabilistically establish the domain stoichiometry using low-resolution information and comparably few particle images.