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3b4a
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(New page: 200px<br /><applet load="3b4a" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b4a, resolution 2.7Å" /> '''T. tengcongensis glmS...)
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Revision as of 09:47, 23 January 2008
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T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate
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
3B4A is a Protein complex structure of sequences from Thermoanaerobacter tengcongensis with and as ligands. 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 Wed Jan 23 11:47:22 2008
