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TitleNMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.
Journal, issue, pagesEur. Biophys. J., Vol. 49, Page 223-230, Year 2020
Publish dateApr 27, 2019 (structure data deposition date)
AuthorsGolubev, A. / Fatkhullin, B. / Gabdulkhakov, A. / Bikmullin, A. / Nurullina, L. / Garaeva, N. / Islamov, D. / Klochkova, E. / Klochkov, V. / Aganov, A. ...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.
External linksEur. Biophys. J. / PubMed:32152681
MethodsX-ray diffraction / NMR (solution)
Resolution1.48 Å
Structure data

PDB-6rji:
X-ray structure of the elongation factor P of S. aureus
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

PDB-6rk3:
Solution structure of the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus
Method: SOLUTION NMR

Chemicals

ChemComp-HOH:
WATER

Source
  • staphylococcus aureus (strain nctc 8325) (bacteria)
  • staphylococcus aureus (bacteria)
KeywordsTRANSLATION / Elongation factor P / EFP / EF-P / STRUCTURAL PROTEIN / Staphylococcus aureus / Ribosome

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