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- W3039596711 abstract "Abstract The ϵ subunit of ATP synthases has been proposed to regulate ATP hydrolysis in bacteria. Prevailing evidence supports the notion that when the ATP concentration falls below a certain threshold, the ϵ subunit changes its conformation from a non‐inhibitory down‐state to an extended up‐state that then inhibits enzymatic ATP hydrolysis by binding to the catalytic domain. It has been demonstrated that the ϵ subunit from Bacillus PS3 is selective for ATP over other nucleotides, including GTP. In this study, the purine triphosphate selectivity is rationalized by using results from MD simulations and free energy calculations for the R103A/R115A mutant of the ϵ subunit from Bacillus PS3, which binds ATP more strongly than the wild‐type protein. Our results are in good agreement with experimental data, and the elucidated molecular basis for selectivity could help to guide the design of novel GTP sensors." @default.
- W3039596711 created "2020-07-10" @default.
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- W3039596711 date "2020-08-04" @default.
- W3039596711 modified "2023-09-30" @default.
- W3039596711 title "The Molecular Basis for Purine Binding Selectivity in the Bacterial ATP Synthase ϵ Subunit" @default.
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- W3039596711 doi "https://doi.org/10.1002/cbic.202000291" @default.
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