488d: Difference between revisions
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==CATALYTIC RNA ENZYME-PRODUCT COMPLEX== | ==CATALYTIC RNA ENZYME-PRODUCT COMPLEX== | ||
<StructureSection load='488d' size='340' side='right' caption='[[488d]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='488d' size='340' side='right' caption='[[488d]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCC:CYTIDINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>CCC</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCC:CYTIDINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>CCC</scene></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=488d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=488d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=488d RCSB], [http://www.ebi.ac.uk/pdbsum/488d PDBsum]</span></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=488d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=488d OCA], [http://pdbe.org/488d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=488d RCSB], [http://www.ebi.ac.uk/pdbsum/488d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=488d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 488d" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 21:59, 10 December 2016
CATALYTIC RNA ENZYME-PRODUCT COMPLEXCATALYTIC RNA ENZYME-PRODUCT COMPLEX
Structural highlights
Publication Abstract from PubMedWe have determined the crystal structure of the enzyme-product complex of the hammerhead ribozyme by using a reinforced crystal lattice to trap the complex prior to dissociation and by employing X-ray holographic image reconstruction, a real-space electron density imaging and refinement procedure. Subsequent to catalysis, the cleavage site residue (C-17), together with its 2',3'-cyclic phosphate, adopts a conformation close to and approximately perpendicular to the Watson-Crick base-pairing faces of two highly conserved purines in the ribozyme's catalytic pocket (G-5 and A-6). We observe several interactions with functional groups on these residues that have been identified as critical for ribozyme activity by biochemical analyses but whose role has defied explanation in terms of previous structural analyses. These interactions may therefore be relevant to the hammerhead ribozyme reaction mechanism. Capture and visualization of a catalytic RNA enzyme-product complex using crystal lattice trapping and X-ray holographic reconstruction.,Murray JB, Szoke H, Szoke A, Scott WG Mol Cell. 2000 Feb;5(2):279-87. PMID:10882069[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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