Summary information and primary citation
- PDB-id
-
2ho6;
SNAP-derived features in text and
JSON formats
- Class
- RNA
- Method
- X-ray (2.8 Å)
- Summary
- Post-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.
