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      Structure, mechanism, and regulation of the chloroplast ATP synthase

      , , , ,
      Science
      American Association for the Advancement of Science (AAAS)

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          Abstract

          The chloroplast ATP synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded F o motor drive ATP synthesis in the F 1 head by rotary catalysis. We determined the high-resolution structure of the complete cF 1 F o complex by cryo-EM, resolving sidechains of all 26 protein subunits, the five nucleotides in the F 1 head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a β-hairpin redox switch in subunit γ that blocks rotation in the dark.

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          Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

          In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.
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            The ATP synthase--a splendid molecular machine.

            P Boyer (1997)
            An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanism with an internal rotation of the gamma subunit. Other structural and mutational probes of the F1 and F0 portions of the ATP synthase are reviewed, together with kinetic and other evaluations of catalytic site occupancy and behavior during hydrolysis or synthesis of ATP. Subunit function as related to proton translocation and rotational catalysis is considered. Physical demonstrations of the gamma subunit rotation have been achieved. The findings have implications for other enzymatic catalyses.
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              Chapter 11 - Reconstitution of membrane proteins in phospholipid bilayer nanodiscs.

              Self-assembled phospholipid bilayer Nanodiscs have become an important and versatile tool among model membrane systems to functionally reconstitute membrane proteins. Nanodiscs consist of lipid domains encased within an engineered derivative of apolipoprotein A-1 scaffold proteins, which can be tailored to yield homogeneous preparations of disks with different diameters, and with epitope tags for exploitation in various purification strategies. A critical aspect of the self-assembly of target membranes into Nanodiscs lies in the optimization of the lipid:protein ratio. Here we describe strategies for performing this optimization and provide examples for reconstituting bacteriorhodopsin as a trimer, rhodopsin, and functionally active P-glycoprotein. Together, these demonstrate the versatility of Nanodisc technology for preparing monodisperse samples of membrane proteins of wide-ranging structure.
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                Author and article information

                Journal
                Science
                Science
                American Association for the Advancement of Science (AAAS)
                0036-8075
                1095-9203
                May 10 2018
                May 11 2018
                May 10 2018
                May 11 2018
                : 360
                : 6389
                : eaat4318
                Article
                10.1126/science.aat4318
                7116070
                29748256
                3e8d615f-232f-4971-96ed-63718dd5276e
                © 2018

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

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