6ZQN

bovine ATP synthase monomer state 3 (combined)

Summary for 6ZQN

• Entry DOI: 10.2210/pdb6zqn/pdb
• Related: 6YY0 6Z1R 6Z1U 6ZBB 6ZG7 6ZG8 6ZIK 6ZIQ 6ZIT 6ZIU 6ZPO 6ZQM
• EMDB information: 11001 11039 11040 11149 11195 11196 11227 11228 11229 11230 11342 11368 11369
• Descriptor: ATP synthase subunit alpha, mitochondrial, ATP synthase subunit a, ATP synthase subunit d, mitochondrial, ... (24 entities in total)
• Functional Keywords: atp synthase, mitochondria, mammalian, complex, hydrolase
• Biological source: Bos taurus (Bovine); More
• Total number of polymer chains: 29
• Total formula weight: 598481.76

Authors

Spikes, T.E.,Montgomery, M.G.,Walker, J.E. (deposition date: 2020-07-10, release date: 2020-09-09, Last modification date: 2020-09-30)

Primary citation

Spikes, T.E.,Montgomery, M.G.,Walker, J.E.
Structure of the dimeric ATP synthase from bovine mitochondria.
Proc.Natl.Acad.Sci.USA, 117:23519-23526, 2020

PubMed Abstract: The structure of the dimeric ATP synthase from bovine mitochondria determined in three rotational states by electron cryo-microscopy provides evidence that the proton uptake from the mitochondrial matrix via the proton inlet half channel proceeds via a Grotthus mechanism, and a similar mechanism may operate in the exit half channel. The structure has given information about the architecture and mechanical constitution and properties of the peripheral stalk, part of the membrane extrinsic region of the stator, and how the action of the peripheral stalk damps the side-to-side rocking motions that occur in the enzyme complex during the catalytic cycle. It also describes wedge structures in the membrane domains of each monomer, where the skeleton of each wedge is provided by three α-helices in the membrane domains of the b-subunit to which the supernumerary subunits e, f, and g and the membrane domain of subunit A6L are bound. Protein voids in the wedge are filled by three specifically bound cardiolipin molecules and two other phospholipids. The external surfaces of the wedges link the monomeric complexes together into the dimeric structures and provide a pivot to allow the monomer-monomer interfaces to change during catalysis and to accommodate other changes not related directly to catalysis in the monomer-monomer interface that occur in mitochondrial cristae. The structure of the bovine dimer also demonstrates that the structures of dimeric ATP synthases in a tetrameric porcine enzyme have been seriously misinterpreted in the membrane domains.

PubMed: 32900941
DOI: 10.1073/pnas.2013998117

Experimental method

ELECTRON MICROSCOPY (4 Å)