(Q54577299)

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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.

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

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. (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

Escherichia coli

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author name string

Watts SD

1

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

Tang C

2

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

Capaldi RA

3

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

language of work or name

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publication date

1 November 1996

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

271

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

45

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

28341-28347

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

The proton-translocating ATPase of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

The binding change mechanism for ATP synthase--some probabilities and possibilities

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Coupling between catalytic sites and the proton channel in F1F0-type ATPases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

The stalk connecting the F1 and F0 domains of ATP synthase visualized by electron microscopy of unstained specimens

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Labeling of the ATP synthase of Escherichia coli from the head-group region of the lipid bilayer

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Components of the mitochondrial inner membrane. 3. Characterization of a seventh different subunit of beef heart cytochrome c oxidase. Similarities between the beef heart enzyme and that from other species

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Monoclonal antibody modification of the ATPase activity of Escherichia coli F1 ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Conformational changes in the Escherichia coli ATP synthase (ECF1F0) monitored by nucleotide-dependent differences in the reactivity of Cys-87 of the gamma subunit in the mutant betaGlu-381 --> Ala.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Nucleotide-dependent movement of the epsilon subunit between alpha and beta subunits in the Escherichia coli F1F0-type ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.45.28341

21 January 2018

Rotation of nucleotide sites is not required for the enzymatic activity of chloroplast coupling factor 1.

1 reference

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21 January 2018

Identifiers

10.1074/JBC.271.45.28341

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/8910457

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