Pre-cleavage state of the Thermoanaerobacter tengcongensis glmS ribozymePre-cleavage state of the Thermoanaerobacter tengcongensis glmS ribozyme

Structural highlights

2gcs is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

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.

See Also

References

  1. Klein DJ, Ferre-D'Amare AR. Structural basis of glmS ribozyme activation by glucosamine-6-phosphate. Science. 2006 Sep 22;313(5794):1752-6. PMID:16990543 doi:313/5794/1752

2gcs, resolution 2.10Å

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