Structural and Functional Insights into the Mode of Action of a Universally Conserved Obg GTPase (original) (raw)
Figure 5
Conserved basic residues in the ObgE-NTD are required for the 50S binding.
(A) Positions of conserved arginine or lysine residues that are subjected to site-directed mutagenesis. (B) Co-sedimentation assay on the binding of various ObgE mutants to the 50S subunit. Wild type (WT) and mutant ObgE (M1–M4) were incubated with equal amount of 50S subunits in the absence or presence of saturating GMPPNP and subjected to co-sedimentation assay. M1, M2, M3, and M4 refer to ObgE mutants, K27EK31E, R76GR82G, R136GR139G, and K27EK31E R76GR82G R136GR139G, respectively.