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3b4a
From Proteopedia
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| - | [[Image:3b4a.gif|left|200px]] | + | [[Image:3b4a.gif|left|200px]] |
| - | + | ||
| - | '''T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate''' | + | {{Structure |
| + | |PDB= 3b4a |SIZE=350|CAPTION= <scene name='initialview01'>3b4a</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3B4A is a [ | + | 3B4A is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermoanaerobacter_tengcongensis Thermoanaerobacter tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B4A OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17990888 17990888] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermoanaerobacter tengcongensis]] | [[Category: Thermoanaerobacter tengcongensis]] | ||
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[[Category: rna]] | [[Category: rna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:56:07 2008'' |
Revision as of 16:56, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 18:56:07 2008
