6RJI
X-ray structure of the elongation factor P of S. aureus
Summary for 6RJI
| Entry DOI | 10.2210/pdb6rji/pdb |
| Descriptor | Elongation factor P (2 entities in total) |
| Functional Keywords | elongation factor p, efp, ef-p, translation |
| Biological source | Staphylococcus aureus (strain NCTC 8325) |
| Total number of polymer chains | 1 |
| Total formula weight | 21403.89 |
| Authors | Fatkhullin, B.F.,Golubev, A.A.,Gabdulkhakov, A.G.,Khusainov, I.S.,Validov, S.Z.,Usachev, K.S.,Yusupova, G.,Yusupov, M.M. (deposition date: 2019-04-27, release date: 2020-04-01, Last modification date: 2024-01-24) |
| 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 Cited by 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: 32152681DOI: 10.1007/s00249-020-01428-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.48 Å) |
Structure validation
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