Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues (Q47954696)

7 February 2018

title

Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues (English)

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7 February 2018

author

Steven B Vik

series ordinal

3

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7 February 2018

author name string

J C Long

series ordinal

1

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7 February 2018

S Wang

series ordinal

2

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7 February 2018

language of work or name

English

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publication date

1 June 1998

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7 February 2018

Journal of Biological Chemistry

published in

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7 February 2018

volume

273

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7 February 2018

issue

26

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7 February 2018

page(s)

16235-16240

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7 February 2018

The ATP synthase--a splendid molecular machine

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Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences.

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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

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Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.

21 January 2018

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Cross-linking of the delta subunit to one of the three alpha subunits has no effect on functioning, as expected if delta is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthase.

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The proton pore in the Escherichia coli F0F1-ATPase: substitution of glutamate by glutamine at position 219 of the alpha-subunit prevents F0-mediated proton permeability

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21 January 2018

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Membrane topology of a cysteine-less mutant of human P-glycoprotein

21 January 2018

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Membrane topology of the di- and tripeptide transport protein of Lactococcus lactis.

21 January 2018

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3-(N-Maleimido-propionyl)biocytin: a versatile thiol-specific biotinylating reagent

21 January 2018

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Assembly of F0 sector of Escherichia coli H+ ATP synthase. Interdependence of subunit insertion into the membrane.

21 January 2018

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Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli.

21 January 2018

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Prediction of transmembrane topology of F0 proteins from Escherichia coli F1F0 ATP synthase using variational and hydrophobic moment analyses.

21 January 2018

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The UNC operon nucleotide sequence, regulation and structure of ATP-synthase

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Intersubunit rotation in active F-ATPase

21 January 2018

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Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

21 January 2018

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Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex

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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The gamma subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part

21 January 2018

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Interaction of the δ and b Subunits Contributes to F1 and F0 Interaction in the Escherichia coli F1F0-ATPase

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.26.16235

1 reference

7 February 2018

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7 February 2018