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Literature summary for 7.1.2.2 extracted from

  • Nakanishi-Matsui, M.; Kashiwagi, S.; Kojima, M.; Nonaka, T.; Futai, M.
    Roles of the beta subunit hinge domain in ATP synthase F1 sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation (2010), Biochem. Biophys. Res. Commun., 395, 173-177.
    View publication on PubMed
Search for more literature for 7.1.2.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain DK8 Escherichia coli

Protein Variants

Protein Variants Comment Organism
betaM159A homology modeling shows a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaS174F, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network suppressing the ATPase activity as well as subunit rotation of betaS174F Escherichia coli
betaM159I homology modeling shows a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaS174F, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network suppressing the ATPase activity as well as subunit rotation of betaS174F Escherichia coli
betaS174F the F1 beta subunit mutation in the hinge domain lowers the gamma subunit rotation speed, and thus decreases the ATPase activity. Homology modeling shows that the amino acid replacement induces a hydrophobic network, in which the Met159, Ile163, and Ala167 residues of the beta subunit are involved together with the mutant betaPhe174, that stabilizes the conformation. Further replacement of betaMet159 with Ala or Ile weakens the hydrophobic network Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphate + H+/out
-
 Escherichia coli ATP + H2O + H+/in
-
 ?
ADP + phosphate + H+/out the ATP synthase beta subunit hinge domain dramatically changes in conformation upon nucleotide binding, overview. The rotation speed of the gamma subunit and the structure of the beta subunit hinge domain are responsible for ATP synthesis activity Escherichia coli ATP + H2O + H+/in
-
 ?

Subunits

Subunits Comment Organism
More the ATP synthase beta subunit hinge domain dramatically changes in conformation upon nucleotide binding, structure and modelling, overview Escherichia coli

Synonyms

Synonyms Comment Organism
ATP synthase F1
-
 Escherichia coli