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      Structure of the ATP synthase catalytic complex (F 1) from Escherichia coli in an auto-inhibited conformation

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      1 , 2
      Nature structural & molecular biology

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          Abstract

          ATP synthase is a membrane-bound, rotary motor enzyme that is critical for cellular energy metabolism in all kingdoms of life. Despite conservation of its basic structure and function, auto-inhibition by one of its rotary stalk subunits occurs in bacteria and chloroplasts but not in mitochondria. The crystal structure of the ATP synthase catalytic complex (F 1) from Escherichia coli described here reveals the structural basis for this inhibition. The C-terminal domain of subunit ε adopts a novel, highly extended conformation that inserts deeply into the central cavity of the enzyme and engages both rotor and stator subunits in extensive contacts that are incompatible with functional rotation. As a result, the three catalytic subunits are stabilized in a set of conformations and rotational positions distinct from previous F 1 structures.

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          Most cited references53

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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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              Escherichia coli acid resistance: tales of an amateur acidophile.

              Gastrointestinal pathogens are faced with an extremely acidic environment. Within moments, a pathogen such as Escherichia coli O157:H7 can move from the nurturing pH 7 environment of a hamburger to the harsh pH 2 milieu of the stomach. Surprisingly, certain microorganisms that grow at neutral pH have elegantly regulated systems that enable survival during excursions into acidic environments. The best-characterized acid-resistance system is found in E. coli.
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                Author and article information

                Journal
                101186374
                31761
                Nat Struct Mol Biol
                Nat. Struct. Mol. Biol.
                Nature structural & molecular biology
                1545-9993
                1545-9985
                24 March 2011
                22 May 2011
                June 2011
                01 December 2011
                : 18
                : 6
                : 701-707
                Affiliations
                [1 ] Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA
                [2 ] Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA
                Author notes
                Correspondence should be addressed to G.C. ( gino.cingolani@ 123456jefferson.edu ) or T.M.D. ( duncant@ 123456upstate.edu )
                Article
                nihpa280997
                10.1038/nsmb.2058
                3109198
                21602818
                6f25cf32-28a0-4a7b-98d0-a8f5beefad9f

                Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms

                History
                Funding
                Funded by: National Institute of General Medical Sciences : NIGMS
                Award ID: R01 GM083088-02 || GM
                Categories
                Article

                Molecular biology
                Molecular biology

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