3i2q
From Proteopedia
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| - | [[ | + | ==Crystal structure of the hairpin ribozyme with 2'OMe substrate strand and N1-deazaadenosine at position A9== |
| + | <StructureSection load='3i2q' size='340' side='right' caption='[[3i2q]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3i2q]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I2Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I2Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1DP:N1-DEAZA-ADENOSINE-5-MONOPHOSPHATE'>1DP</scene>, <scene name='pdbligand=A2M:2-O-METHYLADENOSINE+5-(DIHYDROGEN+PHOSPHATE)'>A2M</scene>, <scene name='pdbligand=S9L:2-[2-(2-HYDROXYETHOXY)ETHOXY]ETHYL+DIHYDROGEN+PHOSPHATE'>S9L</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i2p|3i2p]], [[3i2r|3i2r]], [[3i2s|3i2s]], [[3i2u|3i2u]]</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=3i2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i2q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i2q RCSB], [http://www.ebi.ac.uk/pdbsum/3i2q PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The hairpin ribozyme cleaves a phosphodiester bond within a cognate substrate. Structural and biochemical data indicate the conserved A9 and A10 bases reside close to the scissile bond but make distinct contributions to catalysis. To investigate these residues, we replaced the imino moiety of each base with N1-deazaadenosine. This single-atom change resulted in an 8-fold loss in k(obs) for A9 and displacement of the base from the active site; no effects were observed for A10. We propose that the imino moiety of A9 promotes a key water-mediated contact that favors transition-state formation, which suggests an enhanced chemical repertoire for RNA. | ||
| - | + | Single-atom imino substitutions at A9 and A10 reveal distinct effects on the fold and function of the hairpin ribozyme catalytic core.,Spitale RC, Volpini R, Mungillo MV, Krucinska J, Cristalli G, Wedekind JE Biochemistry. 2009 Aug 25;48(33):7777-9. PMID:19634899<ref>PMID:19634899</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__ |
| - | [[Category: Krucinska, J | + | </StructureSection> |
| - | [[Category: Spitale, R C | + | [[Category: Krucinska, J]] |
| - | [[Category: Wedekind, J E | + | [[Category: Spitale, R C]] |
| + | [[Category: Wedekind, J E]] | ||
[[Category: Hairpin ribozyme]] | [[Category: Hairpin ribozyme]] | ||
[[Category: N1-deazaadenosine]] | [[Category: N1-deazaadenosine]] | ||
[[Category: Rna]] | [[Category: Rna]] | ||
Revision as of 08:48, 8 December 2014
Crystal structure of the hairpin ribozyme with 2'OMe substrate strand and N1-deazaadenosine at position A9
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