3B4C

T. tengcongensis glmS ribozyme bound to glucosamine-6-phosphate and a substrate RNA with a 2'5'-phosphodiester linkage

Summary for 3B4C

Entry DOI	10.2210/pdb3b4c/pdb
Related	3B4A 3B4B
Descriptor	glmS ribozyme substrate with a 2'5'-phosphodiester linkage, glmS ribozyme RNA, 2-amino-2-deoxy-6-O-phosphono-alpha-D-glucopyranose, ... (6 entities in total)
Functional Keywords	ribozyme, riboswitch, glucosamine-6-phosphate, rna
Biological source	Thermoanaerobacter tengcongensis More
Total number of polymer chains	2
Total formula weight	49423.68
Authors	Klein, D.J.,Ferre-D'Amare, A.R. (deposition date: 2007-10-23, release date: 2007-12-11, Last modification date: 2024-02-21)
Primary citation	Klein, D.J.,Been, M.D.,Ferre-D'Amare, A.R. Essential Role of an Active-Site Guanine in glmS Ribozyme Catalysis. J.Am.Chem.Soc., 129:14858-14859, 2007 Cited by PubMed Abstract: The glmS ribozyme is a catalytic riboswitch that is activated for endonucleolytic cleavage by the coenzyme glucosamine-6-phosphate. Using kinetic assays and X-ray crystallography, we identify an active-site mutation of a conserved guanine that abolishes catalysis without perturbing coenzyme binding. Our results provide evidence that coenzyme function requires a specific nucleobase to interact with the nucleophile of the cleavage reaction. PubMed: 17990888 DOI: 10.1021/ja0768441 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3 Å)

Structure validation