Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase. (Q42675708)

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27 January 2020

title

Mechanism of inhibition by C-terminal alpha-helices of the epsilon subunit of Escherichia coli FoF1-ATP synthase (English)

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27 January 2020

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1

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27 January 2020

author name string

Rie Hasegawa

series ordinal

2

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27 January 2020

Kazuhito V Tabata

series ordinal

3

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27 January 2020

Hiroyuki Noji

series ordinal

4

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27 January 2020

language of work or name

English

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publication date

1 May 2009

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Journal of Biological Chemistry

27 January 2020

published in

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27 January 2020

volume

284

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27 January 2020

issue

26

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27 January 2020

page(s)

17457-17464

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Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation

27 January 2020

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27 May 2018

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The role of subunit epsilon in the catalysis and regulation of FOF1-ATP synthase

27 May 2018

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27 May 2018

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27 May 2018

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27 May 2018

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27 May 2018

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27 May 2018

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

27 May 2018

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

27 May 2018

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Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

27 May 2018

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

27 May 2018

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

27 May 2018

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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

27 May 2018

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Structure of the gamma-epsilon complex of ATP synthase

27 May 2018

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The epsilon subunit of bacterial and chloroplast F(1)F(0) ATPases. Structure, arrangement, and role of the epsilon subunit in energy coupling within the complex

27 May 2018

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ATP synthesis by F-type ATP synthase is obligatorily dependent on the transmembrane voltage

27 May 2018

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Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex

27 May 2018

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

27 May 2018

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

27 May 2018

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

27 May 2018

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27 May 2018

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Direct observation of the rotation of F1-ATPase

27 May 2018

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A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions

27 May 2018

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Epsilon subunit of Escherichia coli F1-ATPase: effects on affinity for aurovertin and inhibition of product release in unisite ATP hydrolysis

27 May 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.

27 May 2018

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Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the .epsilon. subunit of Escherichia coli ATP synthase

27 May 2018

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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

27 May 2018

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27 May 2018

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Chemical modification of mono-cysteine mutants allows a more global look at conformations of the epsilon subunit of the ATP synthase from Escherichia coli.

16 August 2018

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16 August 2018

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Stochastic high-speed rotation of Escherichia coli ATP synthase F1 sector: the epsilon subunit-sensitive rotation

16 August 2018

1 reference

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16 August 2018

1 reference

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Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase

16 August 2018

1 reference

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Rotor/Stator interactions of the epsilon subunit in Escherichia coli ATP synthase and implications for enzyme regulation.

16 August 2018

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F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance

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1 reference

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16 August 2018

1 reference

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

16 August 2018

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ATP synthesis by the F1Fo ATP synthase of Escherichia coli is obligatorily dependent on the electric potential

16 August 2018

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12 December 2020

Subunit epsilon of the Escherichia coli ATP synthase: novel insights into structure and function by analysis of thirteen mutant forms

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12 December 2020

Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sites

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12 December 2020

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12 December 2020

The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated

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12 December 2020

Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli

1 reference

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Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins

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12 December 2020

ATP synthesis catalyzed by the ATP synthase of Escherichia coli reconstituted into liposomes

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F1-ATPase rotates by an asymmetric, sequential mechanism using all three catalytic subunits

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12 December 2020

Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80 degrees and 40 degrees substep rotations

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Identifiers

DOI

10.1074/JBC.M109.003798

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19411254%20AND%20SRC:MED&resulttype=core&format=json

27 January 2020

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19411254%20AND%20SRC:MED&resulttype=core&format=json

27 January 2020

PubMed publication ID

19411254

1 reference