6RK3

Solution structure of the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus

Summary for 6RK3

• Entry DOI: 10.2210/pdb6rk3/pdb
• NMR Information: BMRB: 27503
• Descriptor: Elongation factor P (1 entity in total)
• Functional Keywords: ef-p, staphylococcus aureus, ribosome, structural protein
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 20575.01

Authors

Usachev, K.,Fatkhullin, B.,Gabdulkhakov, A.,Khusainov, I.,Golubev, A.,Validov, S.,Yusupova, G.,Yusupov, M. (deposition date: 2019-04-30, release date: 2020-03-11, Last modification date: 2024-05-15)

Primary citation

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.
NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.
Eur.Biophys.J., 49:223-230, 2020

PubMed 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.

PubMed: 32152681
DOI: 10.1007/s00249-020-01428-x

Experimental method

SOLUTION NMR