The role of the betaDELSEED-loop of ATP synthase (Q37160889)

18 August 2017

The role of the betaDELSEED-loop of ATP synthase (English)

1 reference

18 August 2017

Nelli Mnatsakanyan

1

1 reference

18 August 2017

Arathianand M Krishnakumar

series ordinal

2

1 reference

18 August 2017

Toshiharu Suzuki

series ordinal

3

1 reference

18 August 2017

Joachim Weber

series ordinal

4

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18 August 2017

language of work or name

English

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publication date

25 February 2009

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Journal of Biological Chemistry

18 August 2017

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18 August 2017

284

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18 August 2017

17

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18 August 2017

11336-11345

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describes a project that uses

18 August 2017

ImageJ

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2670139/fullTextXML

inferred from PubMed Central ID database lookup

cites work

A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis

1 reference

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A functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase

6 September 2017

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The rotary mechanism of the ATP synthase.

6 September 2017

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Temperature dependence of the rotation and hydrolysis activities of F1-ATPase

6 September 2017

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How subunit coupling produces the gamma-subunit rotary motion in F1-ATPase

6 September 2017

1 reference

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Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site

6 September 2017

1 reference

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Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution

6 September 2017

1 reference

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ATP synthase: subunit-subunit interactions in the stator stalk

6 September 2017

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Catalytic and mechanical cycles in F-ATP synthases. Fourth in the Cycles Review Series

6 September 2017

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A structure-based model for the synthesis and hydrolysis of ATP by F1-ATPase

6 September 2017

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6 September 2017

Rotary molecular motors

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Protein measurement with the Folin phenol reagent

6 September 2017

1 reference

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Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation

6 September 2017

1 reference

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A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F 1 -ATPase

6 September 2017

1 reference

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ATP synthesis driven by proton transport in F1F0-ATP synthase

6 September 2017

1 reference

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Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis

6 September 2017

1 reference

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

6 September 2017

1 reference

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The rotary machine in the cell, ATP synthase

6 September 2017

1 reference

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The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution

6 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

ATP synthase: two motors, two fuels

6 September 2017

1 reference

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Intergenic suppression of the γM23K uncoupling mutation in F0F1 ATP synthase by βGlu-381 substitutions: the role of the β380DELSEED386 segment in energy coupling

6 September 2017

1 reference

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Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied

6 September 2017

1 reference

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

6 September 2017

1 reference

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In vivo evidence for the role of the epsilon subunit as an inhibitor of the proton-translocating ATPase of Escherichia coli

6 September 2017

1 reference

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

6 September 2017

1 reference

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Catalytic Site Nucleotide Binding and Hydrolysis in F1Fo-ATP Synthase

6 September 2017

1 reference

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Adenylate kinase of Escherichia coli: evidence for a functional interaction in phospholipid synthesis

27 June 2018

1 reference

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Purification of F1-ATPase with impaired catalytic activity from partial revertants of Escherichia coli uncA mutant strains

27 June 2018

1 reference

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Oxidative phosphorylation in Escherichia coli. Characterization of mutant strains in which F1-ATPase contains abnormal β-subunits

27 June 2018

1 reference

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Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes

27 June 2018

1 reference

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Further examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit

27 June 2018

1 reference

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Regulatory interplay between proton motive force, ADP, phosphate, and subunit epsilon in bacterial ATP synthase

27 June 2018

1 reference

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The alpha3(betaMet222Ser/Tyr345Trp)3gamma subcomplex of the TF1-ATPase does not hydolyze ATP at a significant rate until the substrate binds to the catalytic site of the lowest affinity

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

The role of the epsilon subunit in the Escherichia coli ATP synthase. The C-terminal domain is required for efficient energy coupling

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

Interactions between beta D372 and gamma subunit N-terminus residues gamma K9 and gamma S12 are important to catalytic activity catalyzed by Escherichia coli F1F0-ATP synthase

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

Highly coupled ATP synthesis by F1-ATPase single molecules

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

ATP synthase that lacks F0a-subunit: isolation, properties, and indication of F0b2-subunits as an anchor rail of a rotating c-ring

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

Fluorescent probes applied to catalytic cooperativity in ATP synthase

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

Origin of apparent negative cooperativity of F(1)-ATPase

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

The beta G156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgAT

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

Expression of the wild-type and the Cys-/Trp-less α3β3γ complex of thermophilic F1-ATPase in Escherichia coli

3 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2670139

F1-ATPase, roles of three catalytic site residues

3 September 2018

1 reference

12 December 2020

Effect of the epsilon-subunit on nucleotide binding to Escherichia coli F1-ATPase catalytic sites

1 reference

12 December 2020

The role of beta-Arg-182, an essential catalytic site residue in Escherichia coli F1-ATPase

1 reference

12 December 2020

A microcolorimetric method for the determination of inorganic phosphorus

1 reference

12 December 2020

Identifiers

DOI

10.1074/JBC.M900374200

1 reference

18 August 2017

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18 August 2017

PubMed publication ID

19246448

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