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. (Q54563780)

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English	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.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

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. (English)

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

Escherichia coli

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author name string

Ogilvie I

1

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

Aggeler R

2

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

Capaldi RA

3

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1 June 2018

http://europepmc.org/abstract/MED/9195980

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publication date

1 June 1997

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

Journal of Biological Chemistry

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PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

272

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

26

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

16652-16656

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

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

1 reference

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

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

1 reference

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

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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.

1 reference

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21 January 2018

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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Characterization of the purified membrane attachment (δ) subunit of the proton translocating adenosine triphosphatase from Escherichia coli

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Escherichia coli H(+)-ATPase: role of the delta subunit in binding Fl to the Fo sector

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Zero-length crosslinking between subunits delta and I of the H(+)-translocating ATPase of chloroplasts

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ATP synthase complex. Proximities of subunits in bovine submitochondrial particles

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Frontiers in ATP synthase research: understanding the relationship between subunit movements and ATP synthesis

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Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase

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Effect of disulfide cross-linking between alpha and delta subunits on the properties of the F1 adenosine triphosphatase of Escherichia coli.

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21 January 2018

Structure-function relationships of domains of the delta subunit in Escherichia coli adenosine triphosphatase.

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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

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21 January 2018

Rapid and efficient site-specific mutagenesis without phenotypic selection

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21 January 2018

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

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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.

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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.

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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

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

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Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of the F1 ATPase from Escherichia coli necessitates revision of the DNA sequence.

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21 January 2018

Solution structure of the N-terminal domain of the delta subunit of the E. coli ATPsynthase

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Cross-linking of engineered subunit delta to (alphabeta)3 in chloroplast F-ATPase.

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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

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Intersubunit rotation in active F-ATPase

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Nuclear matrix and chromosome scaffold preparations of in vitro cultured bovine liver cells have two proteins in common

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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

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Location of Conserved Residue Histidine-38 of the ϵ-Subunit of Escherichia coli ATP Synthase

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Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase

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

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Oligomycin sensitivity conferring protein of mitochondrial ATP synthase: deletions in the N-terminal end cause defects in interactions with F1, while deletions in the C-terminal end cause defects in interactions with F0

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Lack of ability of trypsin-treated mitochondrial F1 -ATPase to bind the oligomycin-sensitivity conferring protein (OSCP)

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Molecular architecture of Escherichia coli F1 adenosinetriphosphatase

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Interconversion of high and low adenosinetriphosphatase activity forms of Escherichia coli F1 by the detergent lauryldimethylamine oxide

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21 January 2018

Identifiers

10.1074/JBC.272.26.16652

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

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1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/9195980

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