Fig. 1: Structure and function of bacterial RNase P. | Nature Communications

Fig. 1: Structure and function of bacterial RNase P.

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

Fig. 1

a RNase P (black arrow) cleaves ptRNA to remove 5′ leader sequences and generate the mature tRNA (green, red, purple). The sequence of 5′ leaders are variable and are optimally single stranded (Sequence A) but can potentially form pairs with the 3′ RCCA (Sequence B) or fold back to form a stem-loop occluding the 5′ leader (Sequence B). b Secondary structure of T. maritima RNase P RNA. c Structure of T. maritima RNase P complex with product tRNA (PDB entry: 3Q1R)10. Zoom-in view for the positioning of the 3′ RCCA sequence. P RNA C-domain is colored purple; the S-domain is orange; L15 region is cyan; rnpA is red; tRNA is gray; 5′ leader is green. d Steps of RNase P catalyzed enzymatic reaction according to Michaelis-Menten mechanism: a substrate S binds reversibly with the enzyme E to form an enzyme-substrate complex ES, subsequently the conformational change introduces the catalytic active ES* state to enable the proceeding of reaction to enzyme-leaving group-product complex, and enzyme E is finally regenerated for the next catalytic cycle.

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