4lmo
From Proteopedia
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| - | + | ==Structure of a vertebrate RNA binding domain of telomerase (TRBD)== | |
| - | + | <StructureSection load='4lmo' size='340' side='right' caption='[[4lmo]], [[Resolution|resolution]] 2.37Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4lmo]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LMO FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r4g|2r4g]], [[3du5|3du5]], [[3du6|3du6]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31033 Takifugu rubripes])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lmo RCSB], [http://www.ebi.ac.uk/pdbsum/4lmo PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Telomerase 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<ref>PMID:24055314</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Takifugu rubripes]] | [[Category: Takifugu rubripes]] | ||
| - | [[Category: Harkisheimer, M | + | [[Category: Harkisheimer, M]] |
| - | [[Category: Mason, M | + | [[Category: Mason, M]] |
| - | [[Category: Shuvaeva, E | + | [[Category: Shuvaeva, E]] |
| - | [[Category: Skordalakes, E | + | [[Category: Skordalakes, E]] |
[[Category: Rna binding domain of the reverse transcriptase telomerase]] | [[Category: Rna binding domain of the reverse transcriptase telomerase]] | ||
[[Category: Rna binding protein]] | [[Category: Rna binding protein]] | ||
Revision as of 15:13, 21 December 2014
Structure of a vertebrate RNA binding domain of telomerase (TRBD)
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