3b4c | pdb_00003b4c

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

spinqualitylabelsall models 3b4c, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b4c is a 2 chain structure with sequence from Thermoanaerobacter tengcongensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3AD, GLP, MG Related: 3b4a, 3b4b Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Essential role of an active-site guanine in glmS ribozyme catalysis.,Klein DJ, Been MD, Ferre-D'Amare AR J Am Chem Soc. 2007 Dec 5;129(48):14858-9. Epub 2007 Nov 9. PMID:17990888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribozyme

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