Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP

Author:

Sobti Meghna12,Ishmukhametov Robert3,Bouwer James C4,Ayer Anita25,Suarna Cacang5,Smith Nicola J26,Christie Mary12,Stocker Roland25,Duncan Thomas M7,Stewart Alastair G12ORCID

Affiliation:

1. Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia

2. St Vincent’s Clinical School, Faculty of Medicine, UNSW Sydney, Sydney, Australia

3. Department of Physics, Clarendon Laboratory, University of Oxford, Oxford, United Kingdom

4. Molecular Horizons, The University of Wollongong, Wollongong, Australia

5. Vascular Biology Division, Victor Chang Cardiac Research Institute, Darlinghurst, Australia

6. Molecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Darlinghurst, Australia

7. Department of Biochemistry & Molecular Biology, SUNY Upstate Medical University, Syracuse, NY, United States

Abstract

ATP synthase produces the majority of cellular energy in most cells. We have previously reported cryo-EM maps of autoinhibited E. coli ATP synthase imaged without addition of nucleotide (Sobti et al. 2016), indicating that the subunit ε engages the α, β and γ subunits to lock the enzyme and prevent functional rotation. Here we present multiple cryo-EM reconstructions of the enzyme frozen after the addition of MgATP to identify the changes that occur when this ε inhibition is removed. The maps generated show that, after exposure to MgATP, E. coli ATP synthase adopts a different conformation with a catalytic subunit changing conformation substantially and the ε C-terminal domain transitioning via an intermediate ‘half-up’ state to a condensed ‘down’ state. This work provides direct evidence for unique conformational states that occur in E. coli ATP synthase when ATP binding prevents the ε C-terminal domain from entering the inhibitory ‘up’ state.

Funder

National Health and Medical Research Council

Biotechnology and Biological Sciences Research Council

Australian Research Council

National Heart Foundation of Australia

Publisher

eLife Sciences Publications, Ltd

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine,General Neuroscience

Reference66 articles.

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