3b4a | pdb_00003b4a
T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate
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| 3b4a, resolution 2.7Å | |||||||||||||
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| Ligands: | A, A23, C, G, GLP, MG, U | ||||||||||||
| Related: | 2z74, 2z75, 2ho7, 3B4B, 3B4C
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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 Mon Mar 31 05:22:55 2008
