5hc9: Difference between revisions
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<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=5hc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hc9 OCA], [http://pdbe.org/5hc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hc9 RCSB], [http://www.ebi.ac.uk/pdbsum/5hc9 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=5hc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hc9 OCA], [http://pdbe.org/5hc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hc9 RCSB], [http://www.ebi.ac.uk/pdbsum/5hc9 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
CCA-adding enzyme adds the 3'-CCA of tRNA, using CTP and ATP as substrates, and terminates RNA synthesis after completion of CCA addition, without using a nucleic acid template. The complex structure of class-II Thermotoga maritima CCA-adding enzyme and mature tRNA with 3'-CCA revealed the mechanisms by which the enzyme terminates RNA synthesis after completion of 3'-CCA addition, and discriminates 3'-mature tRNA from 3'-immature tRNA. After completion of 3'-CCA addition at the catalytic site, the 3'-CCA refolds and relocates to the release site, which is discrete from the catalytic site. The 3'-CCA forms a continuously stacked, stable conformation together with the enzyme. Consequently, the 3'-mature tRNA rotates relative to the surface of the enzyme, and only the 3'-mature tRNA is ready for release. The 3'-regions of immature tRNAs cannot form the stable stacking conformation in the release site; thus, the 3' end is relocated in the catalytic site, and the 3'-CCA is reconstructed. | |||
Mechanism of 3'-Matured tRNA Discrimination from 3'-Immature tRNA by Class-II CCA-Adding Enzyme.,Yamashita S, Tomita K Structure. 2016 Jun 7;24(6):918-25. doi: 10.1016/j.str.2016.03.022. Epub 2016 Apr, 28. PMID:27133023<ref>PMID:27133023</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5hc9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 18:51, 23 June 2016
Thermotoga maritima CCA-adding enzyme complexed with tRNA_CCAThermotoga maritima CCA-adding enzyme complexed with tRNA_CCA
Structural highlights
Publication Abstract from PubMedCCA-adding enzyme adds the 3'-CCA of tRNA, using CTP and ATP as substrates, and terminates RNA synthesis after completion of CCA addition, without using a nucleic acid template. The complex structure of class-II Thermotoga maritima CCA-adding enzyme and mature tRNA with 3'-CCA revealed the mechanisms by which the enzyme terminates RNA synthesis after completion of 3'-CCA addition, and discriminates 3'-mature tRNA from 3'-immature tRNA. After completion of 3'-CCA addition at the catalytic site, the 3'-CCA refolds and relocates to the release site, which is discrete from the catalytic site. The 3'-CCA forms a continuously stacked, stable conformation together with the enzyme. Consequently, the 3'-mature tRNA rotates relative to the surface of the enzyme, and only the 3'-mature tRNA is ready for release. The 3'-regions of immature tRNAs cannot form the stable stacking conformation in the release site; thus, the 3' end is relocated in the catalytic site, and the 3'-CCA is reconstructed. Mechanism of 3'-Matured tRNA Discrimination from 3'-Immature tRNA by Class-II CCA-Adding Enzyme.,Yamashita S, Tomita K Structure. 2016 Jun 7;24(6):918-25. doi: 10.1016/j.str.2016.03.022. Epub 2016 Apr, 28. PMID:27133023[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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