The Subunit delta -Subunit b Domain of the Escherichia coli F1F0 ATPase. THE b SUBUNITS INTERACT WITH F1 AS A DIMER AND THROUGH THE delta SUBUNIT (original ) (raw )The Second Stalk Composed of the b- and delta -subunits Connects F0 to F1 via an alpha -Subunit in the Escherichia coli ATP Synthase
Andrew Rodgers
Journal of Biological Chemistry, 1998
View PDFchevron_right
Nucleotide Binding Drives Conformational Changes in the Isolated α and β Subunits of the F1-ATPase from Escherichia coli
Edgar Contreras
Biochemical and Biophysical Research Communications, 1999
View PDFchevron_right
A Mutation in Which Alanine 128 Is Replaced by Aspartic Acid Abolishes Dimerization of the b-Subunit of the F(0)F(1)-ATPase from Escherichia coli
Andrew Rodgers
Journal of Biological Chemistry, 1996
View PDFchevron_right
Manipulating the Length of the b Subunit F 1 Binding Domain in F 1 F 0 ATP Synthase from Escherichia coli
Tammy Grabar
Journal of Bioenergetics and Biomembranes, 2005
View PDFchevron_right
Formation of a functionally active sodium-translocating hybrid F1F0 ATPase in Escherichia coli by homologous recombination
Georg Kaim
European Journal of Biochemistry, 1993
View PDFchevron_right
Mapping of antigenic sites to monoclonal antibodies on the primary structure of the F1-ATPase β subunit from Escherichia coli: Concealed amino-terminal region of the subunit in the F1
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1992
View PDFchevron_right
The atp operon: nucleotide sequence of the genes for the γ, β, and ε subunits of Escherichia coli ATP synthase
Alex Eberle
Nucleic Acids Research, 1981
View PDFchevron_right
Escherichia coli H+-ATPase: Role of the δ subunit in binding F1 to the F0 sector
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1992
View PDFchevron_right
Molecular genetics of F1-ATPase fromEscherichia coli
Masamitsu Futai
Journal of Bioenergetics and Biomembranes, 1988
View PDFchevron_right
F1TPase of Escherichia coli: A mutation (uncA401) located in the middle of the α subunit affects the conformation essential for F1 activity
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1984
View PDFchevron_right
Role of the amino terminal region of the ϵ subunit of Escherichia coli H+-ATPase (FoF1)
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1992
View PDFchevron_right
Mutations in the conserved proline 43 residue of the uncE protein (subunit c) of Escherichia coli F1F0-ATPase alter the coupling of F1 to F0
Dean Fraga
Journal of Biological Chemistry, 1989
View PDFchevron_right
Solution Structure, Determined by Nuclear Magnetic Resonance, of the b30-82 Domain of Subunit b of Escherichia coli F1Fo ATP Synthase
S. Vivekanandan
Journal of Bacteriology, 2009
View PDFchevron_right
Molecular Mechanism of the ATP Synthase's Fo Motor Probed by Mutational Analyses of Subunit a
Georg Kaim
Journal of Molecular Biology, 2002
View PDFchevron_right
The Dimerization Domain of the b Subunit of the Escherichia coli F1F0-ATPase
Gary Shaw , Stanley Dunn , Derek McLachlin
Journal of Biological Chemistry, 1999
View PDFchevron_right
The ϵ subunit as an ATPase inhibitor of the F1-ATPase in Escherichia coli
Georges Dreyfus
Archives of Biochemistry and Biophysics, 1984
View PDFchevron_right
Dimerization Interactions of the b Subunit of the Escherichia coli F1F0-ATPase
Stanley Dunn , Derek McLachlin
Journal of Biological Chemistry, 1997
View PDFchevron_right
Structure–function relationships in an anion-translocating ATPase
Adrian Walmsley
2000
View PDFchevron_right
Mechanism of F1-ATPase studied by the genetic approach
Masamitsu Futai
Journal of Bioenergetics and Biomembranes, 1988
View PDFchevron_right
F1-ATPase of Escherichia coli: The epsilon-inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands
Tom Duncan
View PDFchevron_right
The b and δ Subunits of the Escherichia coli ATP Synthase Interact via Residues in their C-terminal Regions
Derek McLachlin
Journal of Biological Chemistry, 1998
View PDFchevron_right
Mutational replacements of conserved amino acid residues in the α subunit change the catalytic properties of Escherichia coli F1-ATPase
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1989
View PDFchevron_right
Functional Incorporation of Chimeric b Subunits into F1Fo ATP Synthase
Tammy Grabar
Journal of Bacteriology, 2007
View PDFchevron_right
Identification of α-subunit Lys201 and β-subunit Lys115 at the ATP-binding sites inEscherichia coli F1-ATPase
Masamitsu Futai
FEBS Letters, 1988
View PDFchevron_right
Role of the carboxyl terminal region of H+-ATPase (F0F1 a subunit from Escherichia coli
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1991
View PDFchevron_right
F1-ATPase of Escherichia coli: THE -INHIBITED STATE FORMS AFTER ATP HYDROLYSIS, IS DISTINCT FROM THE ADP-INHIBITED STATE, AND RESPONDS DYNAMICALLY TO CATALYTIC SITE LIGANDS
Tom Duncan
Journal of Biological Chemistry, 2013
View PDFchevron_right
Differential expression of ATPAF1 and ATPAF2 genes encoding F1-ATPase assembly proteins in mouse tissues
Vittoria Petruzzella
FEBS Letters, 2003
View PDFchevron_right
Intracistronic mapping of the defective site and the biochemical properties of β subunit mutants of Escherichia coli H+-ATPase: Correlation of structural domains with functions of the β subunit
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1983
View PDFchevron_right
Complete DNA sequence of the atp operon of the sodium-dependent F1Fo ATP synthase from Ilyobacter tartaricus and identification of the encoded subunits
Georg Kaim
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2003
View PDFchevron_right
Deletion of seven amino acid residues from the γ subunit of Escherichia coli H+-ATPase causes total loss of F1 assembly on membranes
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1985
View PDFchevron_right
Activation and inhibition of the Escherichia coli F1-ATPase by monoclonal antibodies which recognize the ϵ subunit
Richard Tozer , Stanley Dunn
Archives of Biochemistry and Biophysics, 1987
View PDFchevron_right
Understanding ATP synthesis: structure and mechanism of the F1ATPase (Review
J.Alfonso Leyva
Molecular Membrane Biology, 2003
View PDFchevron_right
Escherichia coli H+-ATPase: Loss of the carboxyl terminal region of the γ subunit causes defective assembly of the F1 portion
Masamitsu Futai
Archives of Biochemistry and Biophysics, 1986
View PDFchevron_right
Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data
Duncan McMillan
Open Biology, 2018
View PDFchevron_right
Directed mutagenesis of the strongly conserved lysine 175 in the proposed nucleotide-binding domain of alpha-subunit from Escherichia coli F1-ATPase.
Rajini Rao
Journal of Biological Chemistry, 1988
View PDFchevron_right