Evidence for preorganization of the glmS ribozyme ligand binding pocket.

摘要: We have examined the tertiary structure of ligand-activated glmS ribozyme by a combination methods with aim evaluating magnitude RNA conformational change induced binding cofactor, glucosamine 6-phosphate (GlcN6P). Hydroxyl radical footprinting trans-acting complex identifies several sites solvent protection upon incubation in Mg2+-containing solutions, providing initial evidence fold ribozyme. Under these folding conditions and at GlcN6P concentrations that saturate ligand-induced cleavage reaction, we do not observe changes to this pattern. Cross-linking short-wave UV light yielded similar overall results. In addition, ribozyme−substrate complexes cross-linked absence could be gel purified then activated presence ligand. One active species links base immediately 3‘ site highly conserved region core coul...