3b4a
From Proteopedia
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| - | [[ | + | ==T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate== |
| + | <StructureSection load='3b4a' size='340' side='right' caption='[[3b4a]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3b4a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis Caldanaerobacter subterraneus subsp. tengcongensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B4A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B4A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=A23:ADENOSINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>A23</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z74|2z74]], [[2z75|2z75]], [[2ho7|2ho7]], [[3b4b|3b4b]], [[3b4c|3b4c]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b4a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b4a RCSB], [http://www.ebi.ac.uk/pdbsum/3b4a PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:17990888</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Ribozyme|Ribozyme]] | *[[Ribozyme|Ribozyme]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis]] | ||
[[Category: Amare, A R.Ferre-D.]] | [[Category: Amare, A R.Ferre-D.]] | ||
Revision as of 09:27, 5 November 2014
T. tengcongensis glmS ribozyme with G40A mutation, bound to glucosamine-6-phosphate
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