Fourteen Protomers Compose the Oligomer III of the Proton-rotor in Spinach Chloroplast ATP Synthase (Q50492572)

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scientific article published on October 17, 2003

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English	Fourteen Protomers Compose the Oligomer III of the Proton-rotor in Spinach Chloroplast ATP Synthase	scientific article published on October 17, 2003

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scholarly article

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Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/14529620

Fourteen Protomers Compose the Oligomer III of the Proton-rotor in Spinach Chloroplast ATP Synthase (English)

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18 March 2024

structural biology

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Daniel Jobst Muller

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Daniel J. Müller

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Holger Seelert

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Norbert A. Dencher

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publication date

1 October 2003

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17 October 2003

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Journal of Molecular Biology

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http://europepmc.org/abstract/MED/14529620

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337-344

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Intersubunit rotation in active F-ATPase

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Direct observation of the rotation of F1-ATPase

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Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

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

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The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis

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The structure of the chloroplast F1-ATPase at 3.2 A resolution

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The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide

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The conformation of the epsilon- and gamma-subunits within the Escherichia coli F(1) ATPase

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Molecular architecture of the rotary motor in ATP synthase

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Structural changes linked to proton translocation by subunit c of the ATP synthase

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ATP synthase--a marvellous rotary engine of the cell.

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Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor

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Bacterial Na(+)-ATP synthase has an undecameric rotor

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ATP synthase: constrained stoichiometry of the transmembrane rotor.

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Molecular architecture of the undecameric rotor of a bacterial Na+-ATP synthase

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Structural biology. Proton-powered turbine of a plant motor

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The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.

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Inter-subunit rotation and elastic power transmission in F0F1-ATPase.

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H+/ATP ratio of proton transport-coupled ATP synthesis and hydrolysis catalysed by CF0F1-liposomes

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Arrangement of the multicopy H+-translocating subunit c in the membrane sector of the Escherichia coli F1F0 ATP synthase

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Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis

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Purification of multisubunit membrane protein complexes: isolation of chloroplast FoF1-ATP synthase, CFo and CF1 by blue native electrophoresis

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Dye removal, catalytic activity and 2D crystallization of chloroplast H(+)-ATP synthase purified by blue native electrophoresis

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Detergent effect on anion exchange perfusion chromatography and gel filtration of intact chloroplast H(+)-ATP synthase

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Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM. Atomic force microscopy

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The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids

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Self-assembly of ATP synthase subunit c rings.

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Effects of carbon source on expression of F0 genes and on the stoichiometry of the c subunit in the F1F0 ATPase of Escherichia coli

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The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPase

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Chloroplast F0F1ATP Synthase Imaged by Atomic Force Microscopy

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Dye-ligand chromatographic purification of intact multisubunit membrane protein complexes: application to the chloroplast H+-FoF1-ATP synthase.

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10.1016/J.JMB.2003.08.046

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/14529620

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

14 March 2018

http://europepmc.org/abstract/MED/14529620

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