2004Unpublished venueRequires access

ATP Synthase Stalk Subunits b , δ and ε: Structures and Functions in Energy Coupling

Stanley D. Dunn, Daniel J. Cipriano, P.A. Del Rizzo

Open publisher page 6 citations

Abstract

This chapter contains sections titled: Introduction ε Subunit of ATP Synthase Conformations of the ε Subunit in Crystal Structures of ATP Synthase and the γ′ε Subcomplex ε in the “Down” Conformation ε in the “Up” Conformation Biochemical Analyses of Conformations and Orientations of ε in ATP Synthase Role of the ε Subunit in ATP Synthase Rotation of ε During Hydrolysis Role of ε in the Formation of F1Fo and Inhibition of Soluble F1-ATPase ε as an Inhibitor in ATP Synthase Bidirectional Ratchet Model for ε Function in ATP Synthase Peripheral Stalk of ATP Synthase b Subunit Sequences Structure of E. coli b Membrane-spanning Domain Tether Domain Dimerization Domain δ-Binding Domain Proposed Structural Model of b Structure of δ Interaction of b and δ Position of the Peripheral Stalk in ATP Synthase Function of the Peripheral Stalk Conclusion References

About this research paper

What this paper is about

This chapter contains sections titled: Introduction ε Subunit of ATP Synthase Conformations of the ε Subunit in Crystal Structures of ATP Synthase and the γ′ε Subcomplex ε in the “Down” Conformation ε in the “Up” Conformation Biochemical Analyses of Conformations and Orientations of ε in ATP Synthase Role of the ε Subunit in ATP Synthase Rotation of ε During Hydrolysis Role of ε in the Formation of F1Fo and Inhibition of Soluble F1-ATPase ε as an Inhibitor in ATP Synthase Bidirectional Ratchet Model for ε Function in ATP Synthase Peripheral Stalk of ATP Synthase b Subunit Sequences Structure of E. coli b Membrane-spanning Domain Tether Domain Dimerization Domain δ-Binding Domain Proposed Structural Model of b Structure of δ Interaction of b and δ Position of the Peripheral Stalk in ATP Synthase Function of the Peripheral Stalk Conclusion References

Why it matters

OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

This chapter contains sections titled: Introduction ε Subunit of ATP Synthase Conformations of the ε Subunit in Crystal Structures of ATP Synthase and the γ′ε Subcomplex ε in the “Down” Conformation ε in the “Up” Conformation Biochemical Analyses of Conformations and Orientations of ε in ATP Synthase Role of the ε Subunit in ATP Synthase Rotation of ε During Hydrolysis Role of ε in the Formation of F1Fo and Inhibition of Soluble F1-ATPase ε as an Inhibitor in ATP Synthase Bidirectional Ratchet Model for ε Function in ATP Synthase Peripheral Stalk of ATP Synthase b Subunit Sequences Structure of E. coli b Membrane-spanning Domain Tether Domain Dimerization Domain δ-Binding Domain Proposed Structural Model of b Structure of δ Interaction of b and δ Position of the Peripheral Stalk in ATP Synthase Function of the Peripheral Stalk Conclusion References

Key concepts: ATP synthase, ATP synthase gamma subunit, Stalk, ATP hydrolysis, Protein subunit, V-ATPase, ATPase, Chemistry

Related papers

Back to paper searchBrowse research topicsOriginal source
ATP Synthase Stalk Subunits b , δ and ε: Structures and Functions in Energy Coupling — Research Paper | ScholarLens