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==Telomerase Reverse Transcriptase ternary complex, TERT:DNA:dGpCpp== | ==Telomerase Reverse Transcriptase ternary complex, TERT:DNA:dGpCpp== | ||
<StructureSection load='6usr' size='340' side='right'caption='[[6usr]]' scene=''> | <StructureSection load='6usr' size='340' side='right'caption='[[6usr]], [[Resolution|resolution]] 2.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6USR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6USR FirstGlance]. <br> | <table><tr><td colspan='2'>[[6usr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Red_flour_beetle Red flour beetle]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6USR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6USR FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6usr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6usr OCA], [http://pdbe.org/6usr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6usr RCSB], [http://www.ebi.ac.uk/pdbsum/6usr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6usr ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERT, TcasGA2_TC010963 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7070 Red flour beetle])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6usr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6usr OCA], [http://pdbe.org/6usr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6usr RCSB], [http://www.ebi.ac.uk/pdbsum/6usr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6usr ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Telomerase extends telomere sequences at chromosomal ends to protect genomic DNA. During this process it must select the correct nucleotide from a pool of nucleotides with various sugars and base pairing properties, which is critically important for the proper capping of telomeric sequences by shelterin. Unfortunately, how telomerase selects correct nucleotides is unknown. Here, we determined structures of Tribolium castaneum telomerase reverse transcriptase (TERT) throughout its catalytic cycle and mapped the active site residues responsible for nucleoside selection, metal coordination, triphosphate binding, and RNA template stabilization. We found that TERT inserts a mismatch or ribonucleotide ~1 in 10,000 and ~1 in 14,000 insertion events, respectively. At biological ribonucleotide concentrations, these rates translate to ~40 ribonucleotides inserted per 10 kilobases. Human telomerase assays determined a conserved tyrosine steric gate regulates ribonucleotide insertion into telomeres. Cumulatively, our work provides insight into how telomerase selects the proper nucleotide to maintain telomere integrity. | |||
Mechanisms of nucleotide selection by telomerase.,Schaich MA, Sanford SL, Welfer GA, Johnson SA, Khoang TH, Opresko PL, Freudenthal BD Elife. 2020 Jun 5;9. pii: 55438. doi: 10.7554/eLife.55438. PMID:32501800<ref>PMID:32501800</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6usr" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Telomerase|Telomerase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Freudenthal | [[Category: RNA-directed DNA polymerase]] | ||
[[Category: Schaich | [[Category: Red flour beetle]] | ||
[[Category: Freudenthal, B D]] | |||
[[Category: Schaich, M A]] | |||
[[Category: Nuclear protein]] | |||
[[Category: Polymerase]] | |||
[[Category: Reverse transcriptase]] | |||
[[Category: Telomerase]] | |||
[[Category: Transferase-rna-dna complex]] | |||
Revision as of 12:03, 6 January 2021
Telomerase Reverse Transcriptase ternary complex, TERT:DNA:dGpCppTelomerase Reverse Transcriptase ternary complex, TERT:DNA:dGpCpp
Structural highlights
Publication Abstract from PubMedTelomerase extends telomere sequences at chromosomal ends to protect genomic DNA. During this process it must select the correct nucleotide from a pool of nucleotides with various sugars and base pairing properties, which is critically important for the proper capping of telomeric sequences by shelterin. Unfortunately, how telomerase selects correct nucleotides is unknown. Here, we determined structures of Tribolium castaneum telomerase reverse transcriptase (TERT) throughout its catalytic cycle and mapped the active site residues responsible for nucleoside selection, metal coordination, triphosphate binding, and RNA template stabilization. We found that TERT inserts a mismatch or ribonucleotide ~1 in 10,000 and ~1 in 14,000 insertion events, respectively. At biological ribonucleotide concentrations, these rates translate to ~40 ribonucleotides inserted per 10 kilobases. Human telomerase assays determined a conserved tyrosine steric gate regulates ribonucleotide insertion into telomeres. Cumulatively, our work provides insight into how telomerase selects the proper nucleotide to maintain telomere integrity. Mechanisms of nucleotide selection by telomerase.,Schaich MA, Sanford SL, Welfer GA, Johnson SA, Khoang TH, Opresko PL, Freudenthal BD Elife. 2020 Jun 5;9. pii: 55438. doi: 10.7554/eLife.55438. PMID:32501800[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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