Research Article

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

+ See all authors and affiliations

Science  22 Sep 2006:
Vol. 313, Issue 5794, pp. 1752-1756
DOI: 10.1126/science.1129666

You are currently viewing the abstract.

View Full Text

Abstract

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.

View Full Text

Related Content