(Q54446228)

English

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

scientific article published on 23 February 2007

In more languages

default for all languages

No label defined

No description defined

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

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

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

Escherichia coli

1 reference

based on heuristic

inferred from title

2

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

author name string

Sangeeta Ganti

1

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

publication date

23 February 2007

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

Journal of Bioenergetics and Biomembranes

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

39

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

1

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

99-107

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

Construction and plasmid-borne complementation of strains lacking the epsilon subunit of the Escherichia coli F1F0 ATP synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Delta subunit of rat liver mitochondrial ATP synthase: molecular description and novel insights into the nature of its association with the F1-moiety

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Close proximity of a cytoplasmic loop of subunit a with c subunits of the ATP synthase from Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Epsilon subunit, an endogenous inhibitor of bacterial F(1)-ATPase, also inhibits F(0)F(1)-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mutagenesis of the alpha subunit of the F1Fo-ATPase from Escherichia coli. Mutations at Glu-196, Pro-190, and Ser-199.

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Characterization of the first cytoplasmic loop of subunit a of the Escherichia coli ATP synthase by surface labeling, cross-linking, and mutagenesis

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The carboxyl terminus of the epsilon subunit of the chloroplast ATP synthase is exposed during illumination

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Rotation of the epsilon subunit during catalysis by Escherichia coli FOF1-ATP synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Direct observation of the rotation of epsilon subunit in F1-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Catalytic control and coupling efficiency of the Escherichia coli FoF1 ATP synthase: influence of the Fo sector and epsilon subunit on the catalytic transition state

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structure of the gamma-epsilon complex of ATP synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The nature of the accessible and buried surfaces in proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Function, structure, and biogenesis of mitochondrial ATP synthase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isolated epsilon subunit of thermophilic F1-ATPase binds ATP.

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Alanine-scanning mutagenesis of the epsilon subunit of the F1-F0 ATP synthase from Escherichia coli reveals two classes of mutants.

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Determination of the 1-ethyl-3-[(3-dimethylamino)propyl]-carbodiimide- induced cross-link between the beta and epsilon subunits of Escherichia coli F1-ATPase

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

gammaepsilon Sub-complex of thermophilic ATP synthase has the ability to bind ATP.

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles Review Series

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Purification of membrane attachment and inhibitory subunits of the proton translocating adenosine triphosphatase from Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The gammaepsilon-c subunit interface in the ATP synthase of Escherichia coli. cross-linking of the epsilon subunit to the c subunit ring does not impair enzyme function, that of gamma to c subunits leads to uncoupling

1 reference

https://pubmed.ncbi.nlm.nih.gov/17318395

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1007/S10863-006-9066-6

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/17318395

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q54446228&oldid=2212471120"