ATP binding by an F1Fo ATP synthase ε subunit is pH dependent, suggesting a diversity of ε subunit functional regulation in bacteria
It is a conjecture that the ε subunit regulates ATP hydrolytic function of the F1Fo ATP synthase in bacteria. This has been proposed by the ε subunit taking an extended conformation, with a terminal helix probing into the central architecture of the hexameric catalytic domain, preventing ATP hydroly...
Main Authors: | Alexander Krah, Timothy Vogelaar, Sam I. de Jong, Jolyon K. Claridge, Peter J. Bond, Duncan G. G. McMillan |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2023-02-01
|
Series: | Frontiers in Molecular Biosciences |
Subjects: | |
Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2023.1059673/full |
Similar Items
-
Single mutations in the ε subunit from thermophilic Bacillus PS3 generate a high binding affinity site for ATP
by: Alexander Krah, et al.
Published: (2018-09-01) -
Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data
by: Alexander Krah, et al.
Published: (2018-05-01) -
Bedaquiline Targets the ε Subunit of Mycobacterial F-ATP Synthase
by: Kundu, Subhashri, et al.
Published: (2017) -
The structural basis of a high affinity ATP binding ε subunit from a bacterial ATP synthase.
by: Alexander Krah, et al.
Published: (2017-01-01) -
Cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation
by: Noriyo Mitome, et al.
Published: (2022-02-01)