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Literature summary for 7.1.2.2 extracted from

  • Rees, D.M.; Montgomery, M.G.; Leslie, A.G.; Walker, J.E.
    Structural evidence of a new catalytic intermediate in the pathway of ATP hydrolysis by F1-ATPase from bovine heart mitochondria (2012), Proc. Natl. Acad. Sci. USA, 109, 11139-11143.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
purified mitochondrial membrane F1-ATPase in complex with ADP and Mg2+, 10 mg/ml protein in solution containing 200 mM Tris-DCl, pH 7.2, 400 mM NaCl, and 1 mM ADP, and prepared with D2O, mixed with precipitation solution containing 100 mM Tris-DCl, pH 7.2, 400 mM NaCl, 4 mM MgCl2, 1 mM ADP, and 14% w/v PEG 6000, followed by dialysis against 3 mL of buffer consisting of 100 mM Tris-DCl, pH 8.2, 400 mM NaCl, 4 mM MgCl2, 1 mM ADP, 5 mM phosphorous acid, and 9% w/v PEG 6000 adding PEG is 0.25% steps, room temperature, 1-4 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement and modeling Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane
-
Bos taurus 31966
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Bos taurus
-
ADP + phosphate + H+/out
-
?

Organism

Organism UniProt Comment Textmining
Bos taurus P19483
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
Bos taurus ADP + phosphate + H+/out
-
?
ATP + H2O + H+/in catalytic mechanism of F1-ATPase by structure-function relationship analysis, overview. During hydrolysis of ATP, the rotor turns counterclockwise as viewed from the membrane domain of the intact enzyme in 120 degree steps. Because the rotor is asymmetric, at any moment the three catalytic sites are at different points in the catalytic cycle. One site is devoid of nucleotide and represents a state that has released the products of ATP hydrolysis. A second site has bound the substrate, magnesium. ATP, in a precatalytic state, and in the third site, the substrate is about to undergo hydrolysis Bos taurus ADP + phosphate + H+/out
-
?

Subunits

Subunits Comment Organism
More structure analysis of conformations of the betaE-, betaTP- and betaDP-subunits in ground-state structure of F1-ATPase, catalytic sites and conformational changes, overview Bos taurus

Synonyms

Synonyms Comment Organism
F1-ATPase
-
Bos taurus