Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus.
Fiche publication
Date publication
avril 2019
Journal
Biomolecular NMR assignments
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat
Tous les auteurs :
Blokhin DS, Bikmullin AG, Nurullina LI, Garaeva NS, Validov SZ, Klochkov VV, Aganov AV, Khusainov IS, Yusupov MM, Usachev KS
Lien Pubmed
Résumé
Ribosome binding factor A (RbfA) is a 14.9 kDa adaptive protein of cold shock, which is important for bacterial growth at low temperatures. RbfA can bind to the free 30S ribosomal subunit and interacts with the 5'-terminal helix (helix I) of 16S rRNA. RbfA is important for the efficient processing of 16S rRNA and for the maturation (assembly) of 30S ribosomal subunits. Here we report backbone and side chains H, C and N chemical shift assignments of RbfA from Staphylococcus aureus. Analysis of the backbone chemical shifts by TALOS+ suggests that RbfA contains four α-helixes and three β-strands with α1-β1-β2-α2-α3-β3-α4 topology. Secondary structure of RbfA have KH-domain fold topology with βααβ subunit which is characterized by a helix-kink-helix motif in which the GxxG sequence is replaced by a conserved AxG sequence, where an Ala residue at position 70 forming an interhelical kink. The solution of the structure of this protein factor and its complex with the ribosome by NMR spectroscopy, X-ray diffraction analysis and cryo-electron microscopy will allow further development of highly selective substances for slowing or completely stopping the translation of the pathogenic bacterium S. aureus, which will interfere with the synthesis and isolation of its pathogenicity factors.
Mots clés
Cold shock, Protein NMR, RbfA, Resonance assignment, Ribosome, Staphylococcus aureus
Référence
Biomol NMR Assign. 2019 04;13(1):27-30