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Literature summary for 7.1.2.2 extracted from

  • Motz, C.; Hornung, T.; Kersten, M.; McLachlin, D.T.; Dunn, S.D.; Wise, J.G.; Vogel, P.D.
    The subunit b dimer of the FOF1-ATP synthase: interaction with F1-ATPase as deduced by site-specific spin-labeling (2004), J. Biol. Chem., 279, 49074-49081.
    View publication on PubMed
Search for more literature for 7.1.2.2

Application

Application Comment Organism
additional information site-specific spin-labeling of single cysteine mutations within mutant of subunit b of the ATP-synthase and employed electron spin resonance indicate tight binding interaction between b2 and F1, different binding interactions of b to F1 in the presence or absence of sigma, b preperations spin-labeled between amino acid position 101 and 114 are indicative of either two populations of b subunits with different packing interactions or to helical bending within this region Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information single cysteine mutations of subunit b expressed from Escherichia coli strain JM109 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 and strain JM109
-
Escherichia coli SWM1
-
 and strain JM109
-

Purification (Commentary)

Purification (Comment) Organism
single cysteine mutations of subunit b Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Escherichia coli ADP + phosphate + H+/out
-
 ?
ATP + H2O + H+/in
-
 Escherichia coli SWM1 ADP + phosphate + H+/out
-
 ?

Synonyms

Synonyms Comment Organism
F0F1-ATP synthase
-
 Escherichia coli