Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum
about
The structural basis of a high affinity ATP binding ε subunit from a bacterial ATP synthase.Catalytic robustness and torque generation of the F1-ATPaseDeleting the IF1-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis.Conformational dynamics of the rotary subunit F in the A3 B3 DF complex of Methanosarcina mazei Gö1 A-ATP synthase monitored by single-molecule FRET.ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain and conventional catalytic sites.Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Single mutations in the ε subunit from thermophilic PS3 generate a high binding affinity site for ATP
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Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 12 September 2016
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum
@en
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
@nl
type
label
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum
@en
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
@nl
prefLabel
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum
@en
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
@nl
P2860
P50
P356
P1476
Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum
@en
P2093
Andrew G W Leslie
Gregory M Cook
P2860
P304
10860-10865
P356
10.1073/PNAS.1612035113
P407
P577
2016-09-12T00:00:00Z