5dof
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5dof is ON HOLD until Paper Publication Authors: Wan, B., Tang, T., Wu, J., Lei, M. Description: Crystal structure of Tetrahymena p19 [[Category: U...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Tetrahymena p19== | |
| + | <StructureSection load='5dof' size='340' side='right'caption='[[5dof]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dof]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DOF 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]] 1.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5dof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dof OCA], [https://pdbe.org/5dof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dof RCSB], [https://www.ebi.ac.uk/pdbsum/5dof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dof ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TAP19_TETTS TAP19_TETTS] Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis (PubMed:26551074). Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:26551074). The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis (PubMed:26551074).<ref>PMID:26551074</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tetrahymena telomerase holoenzyme subunits p75, p45 and p19 form a subcomplex (7-4-1) peripheral to the catalytic core. We report structures of p45 and p19 and reveal them as the Stn1 and Ten1 subunits of the CST complex, which stimulates telomerase complementary-strand synthesis. 7-4-1 binds telomeric single-stranded DNA, and mutant p19 overexpression causes telomere 3'-overhang elongation. We propose that telomerase-tethered Tetrahymena CST coordinates telomere G-strand and C-strand synthesis. | ||
| - | + | The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST complex.,Wan B, Tang T, Upton H, Shuai J, Zhou Y, Li S, Chen J, Brunzelle JS, Zeng Z, Collins K, Wu J, Lei M Nat Struct Mol Biol. 2015 Nov 9. doi: 10.1038/nsmb.3126. PMID:26551074<ref>PMID:26551074</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Lei | + | <div class="pdbe-citations 5dof" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: | + | *[[P19|P19]] |
| + | *[[Telomerase-associated protein|Telomerase-associated protein]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tetrahymena thermophila]] | ||
| + | [[Category: Lei M]] | ||
| + | [[Category: Tang T]] | ||
| + | [[Category: Wan B]] | ||
| + | [[Category: Wu J]] | ||
Current revision
Crystal structure of Tetrahymena p19
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