The molecular basis for purine binding selectivity in the bacterial ATP synthase ε subunit.

In this study, the purine triphosphate selectivity is rationalized via results from MD simulations and free energy calculations for the R103A/R115A mutant of the ε subunit from Bacillus PS3, which binds ATP stronger than the wild-type (WT) 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. PMID: 32608105 [PubMed - as supplied by publisher]

https://www.ncbi.nlm.nih.gov/pubmed/32608105?dopt=Abstract

Source: Chembiochem - June 29, 2020 Category: Biochemistry Authors: Krah A, Huber RG, McMillan DGG, Bond PJ Tags: Chembiochem Source Type: research

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