The αβ complexes of ATP synthase: the α3β3 oligomer and α1β1 protomer View Full Text


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Article Info

DATE

1992-10

AUTHORS

Yasuo Kagawa, Shigeo Ohta, Mitsuo Harada, Hiroshi Kihara, Yuji Ito, Mamoru Sato

ABSTRACT

The basic structures of the catalytic portion (F1, alpha 3 beta 3 gamma delta epsilon) of ATP synthase are the alpha 3 beta 3 hexamer (oligomer with cooperativity) and alpha 1 beta 1 heterodimer (protomer). These were reconstituted from the alpha and beta subunits of thermophilic F1 (TF1), and the alpha 3 beta 3 hexamer was crystallized. On electrophoresis, both the dimer and hexamer showed bands with ATPase activity. Using the dimer and hexamer, we studied the nucleotide-dependent rapid molecular dynamics. The formation of the hexamer required neither nucleotide nor Mg. The hexamer was dissociated into the dimer in the presence of MgADP, while the dimer was associated into the hexamer in the presence of MgATP. The hexamer, like mitochondrial F1 and TF1, showed two kinds of ATPase activity: one was cooperative and was inhibited by only one BzADP per hexamer, and the other was inhibited by three BzADP per hexamer. More... »

PAGES

441-445

References to SciGraph publications

  • 1979-08. Structure and function of H+-ATPase in JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
  • 1988-08. ATP synthases—Structure of the F1-moiety and its relationship to function and mechanism in JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
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    http://scigraph.springernature.com/pub.10.1007/bf00762360

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    http://dx.doi.org/10.1007/bf00762360

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1429537


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