Asp residues of βDELSEED-motif are required for peptide binding in the Escherichia coli ATP synthase (original) (raw)

Structure-function relationships of the Escherichia coli ATP synthase probed by trypsin digestion

Marina Gavilanes-Ruíz

Biochemistry, 1988

ε-Binding regions of the γ subunit of Escherichia coli ATP synthase

Stanley Dunn

Residues interacting with serine-174 and alanine-295 in the β-subunit of Escherichia coli H+ATP synthase: Possible ternary structure of the center region of the subunit

Yuri Ishihara

Biochimica Et Biophysica Acta-bioenergetics, 1994

Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase

Sherif Hassan

Archives of biochemistry and biophysics, 2016

doi:10.4061/2011/785741 Review Article Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase

2013

The defective proton-ATPase of uncA mutants of Escherichia coli: ATP-binding and ATP-induced conformational change in mutant [alpha]-subunits

Rajini Rao

Archives of biochemistry and biophysics, 1987

Role of α-Subunit VISIT-DG Sequence Residues Ser-347 and Gly-351 in the Catalytic Sites of Escherichia coli ATP Synthase

Journal of Biological Chemistry, 2009

The defective proton-ATPase of uncA mutants of Escherichia coli: ATP-binding and ATP-induced conformational change in mutant α-subunits

David Perlin

Archives of Biochemistry and Biophysics, 1987

A re-examination of the structural and functional consequences of mutation of alanine-128 of the b subunit of Escherichia coli ATP synthase to aspartic acid

Stanley Dunn

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2000

Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase Article in Archives of Biochemistry and Biophysics · 41 PUBLICATIONS 520 CITATIONS

Sherif Hassan, Zulfiqar Ahmad

Site-directed Cross-linking of b to the α, β, anda Subunits of the Escherichia coli ATP Synthase

Derek McLachlin

Journal of Biological Chemistry, 2000

Role of βAsn-243 in the Phosphate-binding Subdomain of Catalytic Sites of Escherichia coli F1-ATPase

Journal of Biological Chemistry, 2004

Overproduction of truncated subunit a of H+-ATPase causes growth inhibition of Escherichia coli

Journal of Bacteriology, 1989

Letter to the Editor: Backbone 1 H, 15 N and 13 C Assignments for the Subunit a of the E. Coli ATP Synthase

John Markley

J Biomol Nmr, 2004

Characterization of Escherichia coli ATP synthase .beta.-subunit mutations using a chromosomal delection strain

Janet Pagan

Biochemistry, 1991

Escherichia coli ATP synthase (F-ATPase): catalytic site and regulation of H+ translocation

The Journal of experimental biology, 1992

The ϵ subunit as an ATPase inhibitor of the F1-ATPase in Escherichia coli

Georges Dreyfus

Archives of Biochemistry and Biophysics, 1984

Mutational replacements of conserved amino acid residues in the α subunit change the catalytic properties of Escherichia coli F1-ATPase

Archives of Biochemistry and Biophysics, 1989

Identification of phosphate binding residues of Escherichia coli ATP synthase

zaahid ahmad

Journal of bioenergetics and biomembranes, 2005

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

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

The Subunit of the Escherichia coli F1 ATPase Can Be Crosslinked Near the Glycine-rich Loop Region of aSubunit When ADP + Mg2+ Occupies Catalytic Sites but not When ATP + Mg2+ is Bound

Sui Cai

Journal of Biological Chemistry

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

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

Sui Cai

Biochemistry, 1992

Identification of α-subunit Lys201 and β-subunit Lys115 at the ATP-binding sites inEscherichia coli F1-ATPase

FEBS Letters, 1988

Modulation of Charge in the Phosphate Binding Site of Escherichia coli ATP Synthase

Journal of Biological Chemistry, 2005

STRUCTURE AND FUNCTION OF H + -ATPase: WHAT WE HAVE LEARNED FROM Escherichia coli H + -ATPase*

Annals of the New York Academy of Sciences, 1982

The glycine-rich sequence of the beta subunit of Escherichia coli H(+)-ATPase is important for activity

Journal of Biological Chemistry, 1990

Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase

2011

Mutagenesis and reversion analysis of residue MET-209 of the b-subunit of Escherichia coli ATP synth

Janet Pagan

1995

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

Archives of Biochemistry and Biophysics, 1992

The atp operon: nucleotide sequence of the genes for the gamma, beta, and epsilon subunits of Escherichia coli ATP synthase

Alex N. Eberle

Nucleic acids research, 1981

N-Ethylmaleimide-sensitive mutant (βVal-153→Cys)Escherichia coliF1-ATPase: Cross-linking of the mutant β subunit with the α subunit

FEBS Letters, 1994

Tight ATP and ADP binding in the noncatalytic sites of Escherichia coli F1-ATPase is not affected by mutation of bulky residues in the ‘glycine-rich loop’

Janet Pagan

FEBS Letters, 1990