Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site.
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Crystal structure of A3B3 complex of V-ATPase from Thermus thermophilusRegulation of the F0F1-ATP synthase: the conformation of subunit epsilon might be determined by directionality of subunit gamma rotationPurine but not pyrimidine nucleotides support rotation of F(1)-ATPase.Making ATP.The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1-ATPase by the epsilon subunit.Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.One rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolarTemperature dependence of the rotation and hydrolysis activities of F1-ATPaseATP-driven stepwise rotation of FoF1-ATP synthase.The rotary machine in the cell, ATP synthase.A rotary molecular motor that can work at near 100% efficiencyActivation of pausing F1 motor by external forceResolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.Pause and rotation of F(1)-ATPase during catalysisThe rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.Characterization of the relationship between ADP- and epsilon-induced inhibition in cyanobacterial F1-ATPaseε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging.ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilusATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas.The chloroplast ATP synthase features the characteristic redox regulation machinery.Second stalk of ATP synthase. Cross-linking of gamma subunit in F1 to truncated Fob subunit prevents ATP hydrolysis.Chemo-mechanical coupling in F(1)-ATPase revealed by catalytic site occupancy during catalysis.A model of the quaternary structure of the Escherichia coli F1 ATPase from X-ray solution scattering and evidence for structural changes in the delta subunit during ATP hydrolysis.Inhibition of thermophilic F1-ATPase by the ε subunit takes different path from the ADP-Mg inhibition.A conformational change of the γ subunit indirectly regulates the activity of cyanobacterial F1-ATPase.alpha3beta3gamma complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites.Thermodynamic analyses of nucleotide binding to an isolated monomeric β subunit and the α3β3γ subcomplex of F1-ATPaseNeither helix in the coiled coil region of the axle of F1-ATPase plays a significant role in torque production.Severe MgADP inhibition of Bacillus subtilis F1-ATPase is not due to the absence of nucleotide binding to the noncatalytic nucleotide binding sites.Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase.Complete inhibition and partial Re-activation of single F1-ATPase molecules by tentoxin: new properties of the re-activated enzyme.Inverse regulation of rotation of F1-ATPase by the mutation at the regulatory region on the gamma subunit of chloroplast ATP synthase.Real-time monitoring of conformational dynamics of the epsilon subunit in F1-ATPase.Role of the epsilon subunit of thermophilic F1-ATPase as a sensor for ATP.A single mutation at the catalytic site of TF1-alpha3beta3gamma complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity.ATP synthesis by F0F1-ATP synthase independent of noncatalytic nucleotide binding sites and insensitive to azide inhibition.Cross-linking of two beta subunits in the closed conformation in F1-ATPase.The noncatalytic site-deficient alpha3beta3gamma subcomplex and FoF1-ATP synthase can continuously catalyse ATP hydrolysis when Pi is present.Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase.
P2860
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P2860
Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Catalytic activity of the alph ...... lytic nucleotide binding site.
@en
Catalytic activity of the alph ...... lytic nucleotide binding site.
@nl
type
label
Catalytic activity of the alph ...... lytic nucleotide binding site.
@en
Catalytic activity of the alph ...... lytic nucleotide binding site.
@nl
prefLabel
Catalytic activity of the alph ...... lytic nucleotide binding site.
@en
Catalytic activity of the alph ...... lytic nucleotide binding site.
@nl
P2093
P2860
P356
P1476
Catalytic activity of the alph ...... lytic nucleotide binding site.
@en
P2093
P2860
P304
P356
10.1074/JBC.272.13.8215
P407
P577
1997-03-01T00:00:00Z