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Literature summary for 7.1.2.2 extracted from

  • Krah, A.; Pogoryelov, D.; Langer, J.D.; Bond, P.J.; Meier, T.; Faraldo-Gomez, J.D.
    Structural and energetic basis for H+ versus Na+ binding selectivity in ATP synthase Fo rotors (2010), Biochim. Biophys. Acta, 1797, 763-772.
    View publication on PubMed
Search for more literature for 7.1.2.2

Protein Variants

Protein Variants Comment Organism
A63S site-directed mutagenesis, mutation in the c15 rotor reduces its H+ selectivity against Na+, ion coordination and transfer in wild-type enzyme compared to the wild-type enzyme Arthrospira platensis
S66A site-directed mutagenesis, the mutation in the c11 rotor ring increases its proton-binding propensity, consistent with the impaired Na+ binding capacity Arthrospira platensis
S66A/T67L site-directed mutagenesis, the double mutant is in its sequence composition identical to the wild-type c15 rotor, and accordingly it is very highly H+ selective Arthrospira platensis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Arthrospira platensis 16020
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Arthrospira platensis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Arthrospira platensis ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in a distinct glutamate side chain, conserved across all c-subunits of F-ATP synthases, plays a prominent role in ion coordination Arthrospira platensis ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
F1Fo ATP synthase
-
 Arthrospira platensis
H+-coupled ATP synthase
-
 Arthrospira platensis

General Information

General Information Comment Organism
metabolism the coupling of conformational cycle to electrochemical gradient is an efficient means of energy transduction and regulation, for ion binding to the membrane domain, known as Fo, is appropriately selective. H+ selectivity is most likely a robust property of all Fo rotors. In H+-coupled rotors, the incorporation of hydrophobic side chains to the binding sites enhances this inherent H+ selectivity. Size restriction may also favor H+ over Na+, but increasing size alone does not confer Na+ selectivity Arthrospira platensis
additional information molecular dynamics simulations and free-energy calculations of ion coordination and transfer in wild-type enzyme and mutant A63S, overview Arthrospira platensis
physiological function the functional mechanism of the F1Fo ATP synthase entails a conformational cycle that is coupled to the movement of H+ or Na+ ions across its transmembrane domain, down an electrochemical gradient Arthrospira platensis