4eyt: Difference between revisions
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==Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65== | |||
<StructureSection load='4eyt' size='340' side='right'caption='[[4eyt]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4eyt]] is a 6 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=4EYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EYT 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]] 2.5Å</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=4eyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eyt OCA], [https://pdbe.org/4eyt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eyt RCSB], [https://www.ebi.ac.uk/pdbsum/4eyt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eyt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LARP7_TETTS LARP7_TETTS] RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:15131081, PubMed:15696174, PubMed:16507983, PubMed:17322903, PubMed:20713447, PubMed:22315458, PubMed:22705372). 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:15696174, PubMed:17322903, PubMed:20713447). TAP65/p65 specifically binds telomerase RNA template TER and is required for biogenesis and placement of the TER stem-terminus element: TAP65/p65 first protects the 3'-end of TER from degradation and acts as a chaperone to correctly fold TER for protein binding; it then bends TER stem-loop IV to position it for interaction of stem-loop IV with catalytic TERT RNA-binding domain (PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:22315458, PubMed:22705372).<ref>PMID:15131081</ref> <ref>PMID:15696174</ref> <ref>PMID:16507983</ref> <ref>PMID:17322903</ref> <ref>PMID:20713447</ref> <ref>PMID:22315458</ref> <ref>PMID:22705372</ref> | |||
==See Also== | |||
*[[Telomerase-associated protein|Telomerase-associated protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tetrahymena thermophila]] | |||
[[Category: Cascio D]] | |||
[[Category: Collins K]] | |||
[[Category: Feigon J]] | |||
[[Category: Koo B-K]] | |||
[[Category: Patel A]] | |||
[[Category: Singh M]] | |||
[[Category: Wang Z]] |
Latest revision as of 18:12, 14 March 2024
Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65
Structural highlights
FunctionLARP7_TETTS RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex (PubMed:15131081, PubMed:15696174, PubMed:16507983, PubMed:17322903, PubMed:20713447, PubMed:22315458, PubMed:22705372). 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:15696174, PubMed:17322903, PubMed:20713447). TAP65/p65 specifically binds telomerase RNA template TER and is required for biogenesis and placement of the TER stem-terminus element: TAP65/p65 first protects the 3'-end of TER from degradation and acts as a chaperone to correctly fold TER for protein binding; it then bends TER stem-loop IV to position it for interaction of stem-loop IV with catalytic TERT RNA-binding domain (PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:22315458, PubMed:22705372).[1] [2] [3] [4] [5] [6] [7] See AlsoReferences
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