3b4b

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Image:3b4b.gif

Template:STRUCTURE 3b4b

T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate and a substrate RNA with a 2'5'-phosphodiester linkage


Overview

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.

About this Structure

3B4B is a Protein complex structure of sequences from Thermoanaerobacter tengcongensis. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 20:22:50 2008

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