Fig. 2: Structural details of SAMURI postcatalytic core.
From: Structure and catalytic activity of the SAM-utilizing ribozyme SAMURI
a, In the cofactor layer, SeDHA is contacted by G9 and U37 through Watson–Crick interactions with the sugar edge. b, In the reaction layer, the target site A52 forms a base triple with C11•G36. c, In the stabilization layer G10•C34 interacts with U12•A35. d, The bottom layer contains the base triple of C13•G33 and G30. e, Environment of the methionine moiety of SeDHA. f,g, The kink structure around the target site is stabilized by two hydrated magnesium ions. h, Representative excerpt of an in-line probing gel of SAMURI (pH 8.0, 20 °C, 18 h). i, The trans-activity analysis of SAMURI mutants. Reaction conditions: 1 µM Cy5-labeled substrate RNA R1, 10 µM SAMURI wild type (R4) or mutants (R8–R15) (Extended Data Fig. 4 and Supplementary Table 1), 10 µM ProSeDMA, 10 mM MgCl2, 37 °C, 4 h. In h,i, representative gel images are shown from three independent experiments.
