4lmo: Difference between revisions
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==Structure of a vertebrate RNA binding domain of telomerase (TRBD)== | ==Structure of a vertebrate RNA binding domain of telomerase (TRBD)== | ||
<StructureSection load='4lmo' size='340' side='right' caption='[[4lmo]], [[Resolution|resolution]] 2.37Å' scene=''> | <StructureSection load='4lmo' size='340' side='right'caption='[[4lmo]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4lmo]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4lmo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Takifugu_rubripes Takifugu rubripes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LMO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37Å</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=4lmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lmo OCA], [https://pdbe.org/4lmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lmo RCSB], [https://www.ebi.ac.uk/pdbsum/4lmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lmo ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4lmo" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Telomerase 3D structures|Telomerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Takifugu rubripes]] | [[Category: Takifugu rubripes]] | ||
[[Category: Harkisheimer | [[Category: Harkisheimer M]] | ||
[[Category: Mason | [[Category: Mason M]] | ||
[[Category: Shuvaeva | [[Category: Shuvaeva E]] | ||
[[Category: Skordalakes | [[Category: Skordalakes E]] | ||
Latest revision as of 06:12, 21 November 2024
Structure of a vertebrate RNA binding domain of telomerase (TRBD)Structure of a vertebrate RNA binding domain of telomerase (TRBD)
Structural highlights
Publication Abstract from PubMedTelomerase is a ribonucleoprotein reverse transcriptase that replicates the ends of chromosomes, thus maintaining genome stability. Telomerase ribonucleoprotein assembly is primarily mediated by the RNA binding domain (TRBD) of the enzyme. Here we present the high-resolution TRBD structure of the vertebrate, Takifugu rubripes (trTRBD). The structure shows that with the exception of the N-terminal linker, the trTRBD is conserved with the Tribolium castaneum and Tetrahymena thermophila TRBDs, suggesting evolutionary conservation across species. The structure provides a view of the structural organization of the vertebrate-specific VSR motif that binds the activation domain (CR4/5) of the RNA component of telomerase. It also reveals a motif (TFLY) that forms part of the T-CP pocket implicated in template boundary element (TBE) binding. Mutant proteins of conserved residues that consist of part of the T and TFLY motifs disrupt trTRBD-TBE binding and telomerase activity and processivity, supporting an essential role of these motifs in telomerase RNP assembly and function. A Motif in the Vertebrate Telomerase N-Terminal Linker of TERT Contributes to RNA Binding and Telomerase Activity and Processivity.,Harkisheimer M, Mason M, Shuvaeva E, Skordalakes E Structure. 2013 Sep 17. pii: S0969-2126(13)00305-5. doi:, 10.1016/j.str.2013.08.013. PMID:24055314[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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