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2H0W

Post-cleavage state of the Thermoanaerobacter tengcongensis glmS ribozyme

Summary for 2H0W
Entry DOI10.2210/pdb2h0w/pdb
Related2GCS 2GCV 2H0S 2H0X 2H0Z
DescriptorglmS ribozyme product oligonucleotide, glmS ribozyme RNA, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsrna, ribozyme, pseudoknot, helix
Total number of polymer chains2
Total formula weight49365.73
Authors
Klein, D.J.,Ferre-D'Amare, A.R. (deposition date: 2006-05-15, release date: 2006-09-26, Last modification date: 2024-02-14)
Primary citationKlein, D.J.,Ferre-D'Amare, A.R.
Structural basis of glmS ribozyme activation by glucosamine-6-phosphate
Science, 313:1752-1756, 2006
Cited by
PubMed 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.
PubMed: 16990543
DOI: 10.1126/science.1129666
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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