Abstract
Elongation factor P (EF-P) is a translation protein factor that plays an important role in specialized translation of consecutive proline amino acid motifs. EF-P is an essential protein for cell fitness in native environmental conditions. It regulates synthesis of proteins involved in bacterial motility, environmental adaptation and bacterial virulence, thus making EF-P a potential drug target. In the present study, we determined the solution and crystal structure of EF-P from the pathogenic bacteria Staphylococcus aureus at 1.48 Å resolution. The structure can serve as a platform for structure-based drug design of novel antibiotics to combat the growing antibiotic resistance of S. aureus.
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This work was supported by the Russian Science Foundation (Grant 17-74-20009).
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Golubev, A., Fatkhullin, B., Gabdulkhakov, A. et al. NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus. Eur Biophys J 49, 223–230 (2020). https://doi.org/10.1007/s00249-020-01428-x
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DOI: https://doi.org/10.1007/s00249-020-01428-x