3b4c

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|PDB= 3b4c |SIZE=350|CAPTION= <scene name='initialview01'>3b4c</scene>, resolution 3.0&Aring;
|PDB= 3b4c |SIZE=350|CAPTION= <scene name='initialview01'>3b4c</scene>, resolution 3.0&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=3AD:3'-DEOXYADENOSINE'>3AD</scene>
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|LIGAND= <scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=3AD:3&#39;-DEOXYADENOSINE'>3AD</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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[[Category: rna]]
[[Category: rna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:55:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:58:14 2008''

Revision as of 13:58, 23 March 2008


PDB ID 3b4c

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



T. tengcongensis glmS ribozyme 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

3B4C 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

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