Characterization of the Interface between γ and ε Subunits of Escherichia coli F1-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
2. Cross-linking of the gamma subunit of the Escherichia coli ATPase (ECF1) via cysteines introduced by site-directed mutagenesis.
3. Monoclonal antibody modification of the ATPase activity of Escherichia coli F1 ATPase
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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