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Literature summary for 7.1.2.2 extracted from

  • Okuno, D.; Fujisawa, R.; Iino, R.; Hirono-Hara, Y.; Imamura, H.; Noji, H.
    Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation (2008), Proc. Natl. Acad. Sci. USA, 105, 20722-20727.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.2.2

Protein Variants

Protein Variants Comment Organism
E190D the mutation in the beta-subunit reduces the ATP hydrolysis Bacillus sp. (in: Bacteria)
R84C/E190D/E391C incorporating of a single copy of the mutant beta-subunit to construct the chimera F1, alpha3beta2beta(E190D/E391C)gamma(R84C) which shows slowed ATP hydrolysis Bacillus sp. (in: Bacteria)

Inhibitors

Inhibitors Comment Organism Structure
adenosine-5'-(beta,gamma-imino)-triphosphate inhibits F1 rotation Bacillus sp. (in: Bacteria)
azide inhibits F1 rotation Bacillus sp. (in: Bacteria)

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Bacillus sp. (in: Bacteria) 16020
-
mitochondrion
-
 Bacillus sp. (in: Bacteria) 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Bacillus sp. (in: Bacteria)
-
 ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in Bacillus sp. (in: Bacteria) PS3
-
 ADP + phosphate + H+/out
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
-
-
Bacillus sp. (in: Bacteria) PS3
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] structure-function relationship from F1 crystal structure in the stable conformational state, catalytic mechanism, F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state, betaDP is the catalytically active form, overview Bacillus sp. (in: Bacteria)
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in F1-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha3beta3 ring, betaDP is the catalytically active form Bacillus sp. (in: Bacteria) ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in
-
 Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in F1-ATPase is a rotary molecular motor driven by ATP hydrolysis that rotates the gamma-subunit against the alpha3beta3 ring, betaDP is the catalytically active form Bacillus sp. (in: Bacteria) PS3 ADP + phosphate + H+/out
-
 ?
additional information structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview Bacillus sp. (in: Bacteria) ?
-
 ?
additional information structure-function relationship of the R84C/E190D/E391C mutant enzyme, overview Bacillus sp. (in: Bacteria) PS3 ?
-
 ?

Subunits

Subunits Comment Organism
More structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
F1-ATPase
-
 Bacillus sp. (in: Bacteria)

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bacillus sp. (in: Bacteria)