Nucleotide-dependent Movement of the ε Subunit between α and β Subunits in the Escherichia coli F1F0-type ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
2. ATP hydrolysis-linked structural changes in the N-terminal part of the gamma subunit of Escherichia coli F1-ATPase examined by cross-linking studies
3. Labeling of the ATP synthase of Escherichia coli from the head-group region of the lipid bilayer
4. Introduction of reactive cysteine residues in the .epsilon. subunit of Escherichia coli F1 ATPase, modification of these sites with (azidotetrafluorophenyl)maleimides, and examination of changes in the binding of the .epsilon. subunit when different nucleotides are in catalytic sites
5. The gamma subunit of the Escherichia coli F1-ATPase can be cross-linked near the glycine-rich loop region of a beta subunit when ADP + Mg2+ occupies catalytic sites but not when ATP + Mg2+ is bound.
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3. Modulation of coupling in the Escherichia coli ATP synthase by ADP and P i : Role of the ε subunit C-terminal domain;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2017-01
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5. Protein–protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries;Progress in Biophysics and Molecular Biology;2015-10
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