DSSR-PyMOL cartoon-block schematics: PDB entry 2h0s

PDB-id

2h0s; DSSR-derived features in text and JSON formats

Class

RNA

Method

X-ray (2.35 Å)

Summary

Pre-cleavage state of the thermoanaerobacter tengcongensis glms ribozyme

Reference

Klein DJ, Ferre-D'Amare AR (2006): "Structural basis of glmS ribozyme activation by glucosamine-6-phosphate." Science, 313, 1752-1756. doi: 10.1126/science.1129666.

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.