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Science 22 September 2006:
Vol. 313. no. 5794, pp. 1752 - 1756
DOI: 10.1126/science.1129666
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Research Articles

Structural Basis of glmS Ribozyme Activation by Glucosamine-6-Phosphate

Daniel J. Klein and Adrian R. Ferré-D'Amaré*

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.

Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109–1024, USA.

* To whom correspondence should be addressed. E-mail: aferre{at}fhcrc.org

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