Fig. 5: Dynamics of the RNase P holoenzyme and ES complex. | Nature Communications

Fig. 5: Dynamics of the RNase P holoenzyme and ES complex.

From: Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P

Fig. 5: Dynamics of the RNase P holoenzyme and ES complex.The alternative text for this image may have been generated using AI.

a Folding of E. coli RNase P holoenzyme and assembly with various ptRNA substrates. Size-exclusion chromatograms of RNase P holoenzyme in the presence of Mg2+ (top) and AU_ES* and GG_ES* ptRNA-bound complexes assembled in the presence of Ca2+. UV absorbance profile at 260 nm (black line) and 280 nm (red line). Peak fraction under the blue arrow was used for cryoEM study. b Distribution of conformational states observed for RNase P holoenzyme and ptRNA-bound complexes. c Model for molecular recognition of ptRNA by RNase P. A flexible S-domain undergoes a conformational change upon binding ptRNA, which may occur by kinetic trapping or classic induced fit to form an intermediate ES complex. ES undergoes another conformational change to form a stable ES* complex in which the 3′ RCCA of ptRNA base pairs are unwound and the 5′ leader and cleavage site are recognized by the RNase P active site.

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