ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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81 citing papers in PubMed, 144 citations in OpenAlex.
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- I-Shaped Dimers of a Plant Chloroplast FInternational journal of molecular sciences · 2023Article
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- Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase.Nature communications · 2023Article
- Inhibitory to non-inhibitory evolution of theFrontiers in molecular biosciences · 2023Article
- Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IFMicroorganisms · 2022Review
- Computational Design of Inhibitors Targeting the Catalytic β Subunit ofAntibiotics (Basel, Switzerland) · 2022Article
- ATP synthase FCellular and molecular life sciences : CMLS · 2022Review
- CryoEM Reveals the Complexity and Diversity of ATP Synthases.Frontiers in microbiology · 2022Review
- Exploring the druggability of the binding site of aurovertin, an exogenous allosteric inhibitor of FFrontiers in pharmacology · 2022Article
- Structure of the ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2021Article
21 more citing papers are in PubMed but not listed here.
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4 authors at 2 institutions in 1 country.
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Abstract
The structure of the intact ATP synthase from the α-proteobacterium Paracoccus denitrificans, inhibited by its natural regulatory ζ-protein, has been solved by X-ray crystallography at 4.0 Å resolution. The ζ-protein is bound via its N-terminal α-helix in a catalytic interface in the F1 domain. The bacterial F1 domain is attached to the membrane domain by peripheral and central stalks. The δ-subunit component of the peripheral stalk binds to the N-terminal regions of two α-subunits. The stalk extends via two parallel long α-helices, one in each of the related b and b' subunits, down a noncatalytic interface of the F1 domain and interacts in an unspecified way with the a-subunit in the membrane domain. The a-subunit lies close to a ring of 12 c-subunits attached to the central stalk in the F1 domain, and, together, the central stalk and c-ring form the enzyme's rotor. Rotation is driven by the transmembrane proton-motive force, by a mechanism where protons pass through the interface between the a-subunit and c-ring via two half-channels in the a-subunit. These half-channels are probably located in a bundle of four α-helices in the a-subunit that are tilted at ∼30° to the plane of the membrane. Conserved polar residues in the two α-helices closest to the c-ring probably line the proton inlet path to an essential carboxyl group in the c-subunit in the proton uptake site and a proton exit path from the proton release site. The structure has provided deep insights into the workings of this extraordinary molecular machine.
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