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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 2.7&Aring;" /> '''T. tengcongensis glmS...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermoanaerobacter tengcongensis]]
[[Category: Thermoanaerobacter tengcongensis]]
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[[Category: Amare, A.R.Ferre-D.]]
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[[Category: Amare, A R.Ferre-D.]]
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[[Category: Klein, D.J.]]
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[[Category: Klein, D J.]]
[[Category: GLP]]
[[Category: GLP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: rna]]
[[Category: rna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:47:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:03:10 2008''

Revision as of 17:03, 21 February 2008


3b4a, resolution 2.7Å

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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 Thu Feb 21 19:03:10 2008

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