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4o26
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4o26 is ON HOLD Authors: Huang, J., Wu, J., Lei, M. Description: Crystal structure of the TRBD domain of TERT and the CR4/5 of TR) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the TRBD domain of TERT and the CR4/5 of TR== | |
| + | <StructureSection load='4o26' size='340' side='right'caption='[[4o26]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4o26]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryzias_latipes Oryzias latipes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O26 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.001Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4o26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o26 OCA], [https://pdbe.org/4o26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o26 RCSB], [https://www.ebi.ac.uk/pdbsum/4o26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o26 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TERT_ORYLA TERT_ORYLA] Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.<ref>PMID:18039659</ref> <ref>PMID:22123986</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR. | ||
| - | + | Structural basis for protein-RNA recognition in telomerase.,Huang J, Brown AF, Wu J, Xue J, Bley CJ, Rand DP, Wu L, Zhang R, Chen JJ, Lei M Nat Struct Mol Biol. 2014 Jun;21(6):507-12. doi: 10.1038/nsmb.2819. Epub 2014 May, 4. PMID:24793650<ref>PMID:24793650</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4o26" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Telomerase 3D structures|Telomerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryzias latipes]] | ||
| + | [[Category: Huang J]] | ||
| + | [[Category: Lei M]] | ||
| + | [[Category: Wu J]] | ||
Current revision
Crystal structure of the TRBD domain of TERT and the CR4/5 of TR
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