488d: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[488d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=488D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=488D FirstGlance]. <br> | <table><tr><td colspan='2'>[[488d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=488D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=488D FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCC:CYTIDINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>CCC</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=488d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=488d OCA], [https://pdbe.org/488d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=488d RCSB], [https://www.ebi.ac.uk/pdbsum/488d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=488d ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=488d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=488d OCA], [https://pdbe.org/488d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=488d RCSB], [https://www.ebi.ac.uk/pdbsum/488d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=488d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Murray | [[Category: Murray JB]] | ||
[[Category: Scott | [[Category: Scott WG]] | ||
[[Category: Szoke | [[Category: Szoke A]] | ||
[[Category: Szoke | [[Category: Szoke H]] | ||
Latest revision as of 03:35, 28 December 2023
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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