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      Atomic model for the dimeric FOregion of mitochondrial ATP synthase

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      American Association for the Advancement of Science (AAAS)

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          Abstract

          Mitochondrial ATP synthase produces the majority of ATP in eukaryotic cells and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded FO region turns the rotor that drives ATP synthesis in the soluble F1 region. While crystal structures of the F1 region have illustrated how rotation leads to ATP synthesis, the lack of an experimental atomic model for the FO region has prevented understanding how proton translocation produces rotation. We determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at 3.6 Å resolution by electron cryomicroscopy. The structure reveals the proton path through the complex, how the complex dimerizes, and suggests how it bends the membrane to produce cristae.

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          The operated Markov´s chains in economy (discrete chains of Markov with the income)

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            BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.

            The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
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              The ATP synthase: the understood, the uncertain and the unknown.

              The ATP synthases are multiprotein complexes found in the energy-transducing membranes of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive force, Δp, as a source of energy to drive a mechanical rotary mechanism that leads to the chemical synthesis of ATP from ADP and Pi. Their overall architecture, organization and mechanistic principles are mostly well established, but other features are less well understood. For example, ATP synthases from bacteria, mitochondria and chloroplasts differ in the mechanisms of regulation of their activity, and the molecular bases of these different mechanisms and their physiological roles are only just beginning to emerge. Another crucial feature lacking a molecular description is how rotation driven by Δp is generated, and how rotation transmits energy into the catalytic sites of the enzyme to produce the stepping action during rotation. One surprising and incompletely explained deduction based on the symmetries of c-rings in the rotor of the enzyme is that the amount of energy required by the ATP synthase to make an ATP molecule does not have a universal value. ATP synthases from multicellular organisms require the least energy, whereas the energy required to make an ATP molecule in unicellular organisms and chloroplasts is higher, and a range of values has been calculated. Finally, evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria. Here the enzymes form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae.
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                Author and article information

                Journal
                Science
                Science
                American Association for the Advancement of Science (AAAS)
                0036-8075
                1095-9203
                November 16 2017
                November 17 2017
                November 17 2017
                October 26 2017
                : 358
                : 6365
                : 936-940
                Article
                10.1126/science.aao4815
                6402782
                29074581
                d6355fe0-c450-4662-9fe6-d6a35f2f37a2
                © 2017

                http://www.sciencemag.org/about/science-licenses-journal-article-reuse

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