Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Klein DJ, Been MD, Ferre-D'Amare AR. Essential role of an active-site guanine in glmS ribozyme catalysis. J Am Chem Soc. 2007 Dec 5;129(48):14858-9. Epub 2007 Nov 9. PMID:17990888 doi:10.1021/ja0768441
