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The glmS ribozyme is the only natural catalytic RNA known to require a small-molecule activator for catalysis. This catalytic RNA functions as a riboswitch, with activator-dependent RNA cleavage regulating glmS messenger RNA expression. We report crystal structures of the glmS ribozyme in precleavage states that are unliganded or bound to the competitive inhibitor glucose-6-phosphate and in the postcleavage state. All structures superimpose closely, revealing a remarkably rigid RNA that contains a preformed active and coenzyme-binding site. Unlike other riboswitches, the glmS ribozyme binds its activator in an open, solvent-accessible pocket. Our structures suggest that the amine group of the glmS ribozyme-bound coenzyme performs general acid-base and electrostatic catalysis.
Structural basis of glmS ribozyme activation by glucosamine-6-phosphate.,Klein DJ, Ferre-D'Amare AR Science. 2006 Sep 22;313(5794):1752-6. PMID:16990543[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
