Please use this identifier to cite or link to this item: https://doi.org/10.7717/peerj.5505
Title: Single mutations in the ε subunit from thermophilic Bacillus PS3 generate a high binding affinity site for ATP
Authors: Krah A.
Bond P.J. 
Keywords: ATP binding
ATP synthase
Binding affinity
MD simulations
ε subunit
Issue Date: 2018
Publisher: PeerJ Inc.
Citation: Krah A., Bond P.J. (2018). Single mutations in the ε subunit from thermophilic Bacillus PS3 generate a high binding affinity site for ATP. PeerJ 2018 (9) : e5505. ScholarBank@NUS Repository. https://doi.org/10.7717/peerj.5505
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 mM 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. © 2018 Krah and Bond.
Source Title: PeerJ
URI: http://scholarbank.nus.edu.sg/handle/10635/152046
ISSN: 21678359
DOI: 10.7717/peerj.5505
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