2mhi
From Proteopedia
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(New page: '''Unreleased structure''' The entry 2mhi is ON HOLD Authors: Kim, N., Zhang, Q., Feigon, J. Description: Hold for publication) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of the CR4/5 domain of medaka telomerase RNA== | |
| + | <StructureSection load='2mhi' size='340' side='right'caption='[[2mhi]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2mhi]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHI FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhi OCA], [https://pdbe.org/2mhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhi RCSB], [https://www.ebi.ac.uk/pdbsum/2mhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Telomerase is a unique reverse transcriptase that maintains the 3' ends of eukaryotic chromosomes by adding tandem telomeric repeats. The RNA subunit (TR) of vertebrate telomerase provides a template for reverse transcription, contained within the conserved template/pseudoknot domain, and a conserved regions 4 and 5 (CR4/5) domain, all essential for catalytic activity. We report the nuclear magnetic resonance (NMR) solution structure of the full-length CR4/5 domain from the teleost fish medaka (Oryzias latipes). Three helices emanate from a structured internal loop, forming a Y-shaped structure, where helix P6 stacks on P5 and helix P6.1 points away from P6. The relative orientations of the three helices are Mg2+ dependent and dynamic. Although the three-way junction is structured and has unexpected base pairs, telomerase activity assays with nucleotide substitutions and deletions in CR4/5 indicate that none of these are essential for activity. The results suggest that the junction is likely to change conformation in complex with telomerase reverse transcriptase and that it provides a flexible scaffold that allows P6 and P6.1 to correctly fold and interact with telomerase reverse transcriptase. | ||
| - | + | Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function.,Kim NK, Zhang Q, Feigon J Nucleic Acids Res. 2013 Dec 11. PMID:24335084<ref>PMID:24335084</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2mhi" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Telomerase 3D structures|Telomerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Feigon J]] | ||
| + | [[Category: Kim N]] | ||
| + | [[Category: Zhang Q]] | ||
Current revision
Solution structure of the CR4/5 domain of medaka telomerase RNA
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