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• W2890900258 endingPage "e5505" @default.
• W2890900258 startingPage "e5505" @default.
• W2890900258 abstract "The ε subunit from ATP synthases acts as an ATP sensor in the bacterial cell to prevent ATP hydrolysis and thus the waste of ATP under conditions of low ATP concentration. However, the ATP binding affinities from various bacterial organisms differ markedly, over several orders of magnitude. For example, the ATP synthases from thermophilic Bacillus PS3 and Escherichia coli exhibit affinities of 4 µM and 22 mM, respectively. The recently reported R103A/R115A double mutant of Bacillus PS3 ATP synthase demonstrated an increased binding affinity by two orders of magnitude with respect to the wild type. Here, we used atomic-resolution molecular dynamics simulations to determine the role of the R103A and R115A single mutations. These lead us to predict that both single mutations also cause an increased ATP binding affinity. Evolutionary analysis reveals R103 and R115 substitutions in the ε subunit from other bacillic organisms, leading us to predict they likely have a higher ATP binding affinity than previously expected." @default.
• W2890900258 created "2018-09-27" @default.
• W2890900258 creator A5001674990 @default.
• W2890900258 creator A5087764250 @default.
• W2890900258 date "2018-09-05" @default.
• W2890900258 modified "2023-09-25" @default.
• W2890900258 title "Single mutations in the ε subunit from thermophilic <i>Bacillus</i> PS3 generate a high binding affinity site for ATP" @default.
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• W2890900258 doi "https://doi.org/10.7717/peerj.5505" @default.
• W2890900258 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6129141" @default.
• W2890900258 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30202650" @default.
• W2890900258 hasPublicationYear "2018" @default.
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