301d: Difference between revisions
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<StructureSection load='301d' size='340' side='right'caption='[[301d]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='301d' size='340' side='right'caption='[[301d]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[301d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=301D OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[301d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=301D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=301D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=301d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=301d OCA], [https://pdbe.org/301d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=301d RCSB], [https://www.ebi.ac.uk/pdbsum/301d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=301d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Ribozyme|Ribozyme]] | *[[Ribozyme 3D structures|Ribozyme 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:23, 4 May 2022
CAPTURING THE STRUCTURE OF A CATALYTIC RNA INTERMEDIATE: RNA HAMMERHEAD RIBOZYME, MG(II)-SOAKEDCAPTURING THE STRUCTURE OF A CATALYTIC RNA INTERMEDIATE: RNA HAMMERHEAD RIBOZYME, MG(II)-SOAKED
Structural highlights
Publication Abstract from PubMedThe crystal structure of an unmodified hammerhead RNA in the absence of divalent metal ions has been solved, and it was shown that this ribozyme can cleave itself in the crystal when divalent metal ions are added. This biologically active RNA fold is the same as that found previously for two modified hammerhead ribozymes. Addition of divalent cations at low pH makes it possible to capture the uncleaved RNA in metal-bound form. A conformational intermediate, having an additional Mg(II) bound to the cleavage-site phosphate, was captured by freeze-trapping the RNA at an active pH prior to cleavage. The most significant conformational changes were limited to the active site of the ribozyme, and the changed conformation requires only small additional movements to reach a proposed transition-state. Capturing the structure of a catalytic RNA intermediate: the hammerhead ribozyme.,Scott WG, Murray JB, Arnold JR, Stoddard BL, Klug A Science. 1996 Dec 20;274(5295):2065-9. PMID:8953035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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