Journal
CHEMBIOCHEM
Volume 21, Issue 22, Pages 3249-3254Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202000291
Keywords
ATP synthase; BacillusPS3; epsilon subunit; ligand selectivity; molecular dynamics simulations
Funding
- BII (A*STAR)
- TU Delft StartUP fund
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The epsilon 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 epsilon 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 epsilon subunit fromBacillusPS3 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 epsilon subunit fromBacillusPS3, 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.
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