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

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Golubev, Aleksandr | Fatkhullin, Bulat | Gabdulkhakov, Azat | Bikmullin, Aydar | Nurullina, Liliya | Garaeva, Natalia | Islamov, Daut | Klochkova, Evelina | Klochkov, Vladimir | Aganov, Albert | Khusainov, Iskander | Validov, Shamil | Yusupova, Gulnara | Yusupov, Marat | Usachev, Konstantin

Edité par CCSD ; Springer Verlag (Germany) -

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 A 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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