Single mutations in the ε subunit from thermophilic Bacillus PS3 generate a high binding affinity site for ATP
| Autor: | Peter J. Bond, Alexander Krah |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Protein subunit lcsh:Medicine medicine.disease_cause ATP binding General Biochemistry Genetics and Molecular Biology Bacterial cell structure 03 medical and health sciences ATP hydrolysis medicine Escherichia coli MD simulations ATP synthase biology Chemistry General Neuroscience Thermophile lcsh:R Wild type General Medicine Orders of magnitude (mass) 030104 developmental biology Binding affinity Biochemistry biology.protein General Agricultural and Biological Sciences ε subunit |
| Zdroj: | PeerJ, Vol 6, p e5505 (2018) |
| ISSN: | 2167-8359 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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