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Backbone and side chain NMR assignments for the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus
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Elongation Factor P (EF-P) is a 20.5 kDa protein that provides specialized translation of special stalling amino acid motifs. Proteins with stalling motifs are often involved in various processes, including stress resistance and virulence. Thus it has been shown that the virulent properties of microorganisms can be significantly reduced if the work of EF-P is disrupted. In order to elucidate the structure, dynamics and function of EF-P from Staphylococcus aureus (S. aureus), here we report backbone and side chains (1)H, (13)C and (15)N chemical shift assignments of EF-P. Analysis of the backbone chemical shifts by TALOS+ suggests that EF-P contains 1 alpha-helix and 13 beta-strands (beta1-beta2-beta3-beta4-beta5-beta6-beta7-alpha1-beta8-beta9-beta10-beta11-beta1 2-beta13). The solution of the structure of this protein by NMR and X-ray diffraction analysis, as well as the structure of the ribosome complex by cryo-electron microscopy, will allow further screening of highly selective inhibitors of the translation of the pathogenic bacterium S. aureus. Here we report the almost complete (1)H, (13)C, (15)N backbone and side chain NMR assignment of a 20.5 kDa EF-P.
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