4erd: Difference between revisions
New page: '''Unreleased structure''' The entry 4erd is ON HOLD Authors: Singh, Mahavir, Wang, Zhonghua, Koo, Bon-Kyung, Patel, Anooj, Cascio, Duilio, Collins, Kathleen, Feigon, Juli Description: |
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The | ==Crystal structure of the C-terminal domain of Tetrahymena telomerase protein p65 in complex with stem IV of telomerase RNA== | ||
<StructureSection load='4erd' size='340' side='right'caption='[[4erd]], [[Resolution|resolution]] 2.59Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4erd]] 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=4ERD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ERD 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]] 2.589Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <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=4erd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4erd OCA], [https://pdbe.org/4erd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4erd RCSB], [https://www.ebi.ac.uk/pdbsum/4erd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4erd 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Telomerase is a ribonucleoprotein complex essential for maintenance of telomere DNA at linear chromosome ends. The catalytic core of Tetrahymena telomerase comprises a ternary complex of telomerase RNA (TER), telomerase reverse transcriptase (TERT), and the essential La family protein p65. NMR and crystal structures of p65 C-terminal domain and its complex with stem IV of TER reveal that RNA recognition is achieved by a combination of single- and double-stranded RNA binding, which induces a 105 degrees bend in TER. The domain is a cryptic, atypical RNA recognition motif with a disordered C-terminal extension that forms an alpha helix in the complex necessary for hierarchical assembly of TERT with p65-TER. This work provides the first structural insight into biogenesis and assembly of TER with a telomerase-specific protein. Additionally, our studies define a structurally homologous domain (xRRM) in genuine La and LARP7 proteins and suggest a general mode of RNA binding for biogenesis of their diverse RNA targets. | |||
Structural Basis for Telomerase RNA Recognition and RNP Assembly by the Holoenzyme La Family Protein p65.,Singh M, Wang Z, Koo BK, Patel A, Cascio D, Collins K, Feigon J Mol Cell. 2012 Jun 14. PMID:22705372<ref>PMID:22705372</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4erd" style="background-color:#fffaf0;"></div> | |||
==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]] | |||