Direct observation of the rotation of epsilon subunit in F1-ATPase (Q32050424)

5 July 2017

title

Direct observation of the rotation of epsilon subunit in F1-ATPase (English)

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5 July 2017

Kato-Yamada Y

1

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5 July 2017

Noji H

2

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5 July 2017

Yasuda R

3

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5 July 2017

Kinosita K Jr

4

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5 July 2017

Yoshida M

5

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5 July 2017

language of work or name

English

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publication date

1 July 1998

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Journal of Biological Chemistry

5 July 2017

published in

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5 July 2017

volume

273

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5 July 2017

issue

31

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5 July 2017

page(s)

19375-19377

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ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches

5 July 2017

cites work

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Expression of the wild-type and the Cys-/Trp-less α3β3γ complex of thermophilic F1-ATPase in Escherichia coli

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Structural asymmetry of F1-ATPase caused by the gamma subunit generates a high affinity nucleotide binding site

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

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Direct observation of the rotation of F1-ATPase

21 January 2018

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F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps

21 January 2018

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Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli

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Inhibitory properties of endogenous subunit ϵ in the Escherichia coli F1 ATPase

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Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy

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Crystal structure of the ϵ subunit of the proton-translocating ATP synthase from Escherichia coli

21 January 2018

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The regulatory functions of the gamma and epsilon subunits from chloroplast CF1 are transferred to the core complex, alpha3beta3, from thermophilic bacterial F1.

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Epsilon-binding regions of the gamma subunit of Escherichia coli ATP synthase.

21 January 2018

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Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex.

21 January 2018

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Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.

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Arrangement of the epsilon subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit.

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Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nuc

21 January 2018

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The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

21 January 2018

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Intersubunit rotation in active F-ATPase

21 January 2018

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Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase

21 January 2018

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Cross-linking of chloroplast F0F1-ATPase subunit epsilon to gamma without effect on activity. Epsilon and gamma are parts of the rotor

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.31.19375

1 reference

5 July 2017

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