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Default NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.

NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.

Related Articles NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.

Eur Biophys J. 2020 Mar 09;:

Authors: Golubev A, Fatkhullin B, Gabdulkhakov A, Bikmullin A, Nurullina L, Garaeva N, Islamov D, Klochkova E, Klochkov V, Aganov A, Khusainov I, Validov S, Yusupova G, Yusupov M, Usachev K

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.


PMID: 32152681 [PubMed - as supplied by publisher]



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