A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation. (Q33933707)

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7 November 2019

review article

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title

A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation (English)

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7 November 2019

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1

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7 November 2019

author name string

J C Long

series ordinal

2

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7 November 2019

T Wada

series ordinal

3

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7 November 2019

D Zhang

series ordinal

4

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7 November 2019

language of work or name

English

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publication date

1 May 2000

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Biochimica et Biophysica Acta

7 November 2019

published in

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7 November 2019

volume

1458

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7 November 2019

issue

2-3

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7 November 2019

page(s)

457-466

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The ATP synthase--a splendid molecular machine

7 November 2019

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7 January 2021

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7 January 2021

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Overproduction of truncated subunit a of H+-ATPase causes growth inhibition of Escherichia coli

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7 January 2021

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

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Glutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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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

7 January 2021

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7 January 2021

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

7 January 2021

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Energy transduction in the F1 motor of ATP synthase

7 January 2021

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The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained

7 January 2021

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Energy transduction in ATP synthase

7 January 2021

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Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit

7 January 2021

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The mechanism of ATP synthase: a reassessment of the functions of the b and a subunits

7 January 2021

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Topological studies suggest that the pathway of the protons through F0 is provided by amino acid residues accessible from the lipid phase

7 January 2021

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Voltage-generated torque drives the motor of the ATP synthase

7 January 2021

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Reconstitution of the Fo complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit c after purification in organic solvent.

7 January 2021

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ATP synthase: a tentative structural model

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atp Mutants of Escherichia coli fail to grow on succinate due to a transport deficiency.

7 January 2021

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7 January 2021

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Identifiers

DOI

10.1016/S0005-2728(00)00094-3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10838058%20AND%20SRC:MED&resulttype=core&format=json

7 November 2019

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