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. 2017 Mar;23(3):355–364. doi: 10.1261/rna.059824.116

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Published by Cold Spring Harbor Laboratory Press for the RNA Society.

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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FIGURE 8. — glmS^Ca co-opts a preexisting structural cation for activity. (A) The glmS^AAA active site (Lau and Ferré-D'Amaré 2013). NBPOs with strong and moderate phosphorothioate interference are in red and pink, respectively. Scissile phosphate is in black (*). Residue (−1) is modeled (Lau and Ferré-D'Amaré 2013). (B) Phosphorothioate interferences in glmS^Ca mapped onto the glmS^AAA structure. Residues that differ between glmS^WT and glmS^Ca are in green. (C) Effect of NBPO sulfur substitutions on glmS^Ca. Substitutions of G3 serve as a quality control on the assembly of phosphorothioate-containing ribozymes. Activities of unsubstituted glmS^Ca, pro-Rp, and pro-Sp NBPO substitutions, and diastereomeric substitutions are in gray, yellow, purple, and orange, respectively. Sr²⁺ activities are shown in brown. (*), (**), and (***) denote 0.05 < P < 0.01, 0.001 < P < 0.01, and P < 0.001, respectively (two-tailed t-test).