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| | <StructureSection load='2b2a' size='340' side='right'caption='[[2b2a]], [[Resolution|resolution]] 2.22Å' scene=''> | | <StructureSection load='2b2a' size='340' side='right'caption='[[2b2a]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2b2a]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetth Tetth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B2A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b2a]] is a 3 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=2B2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B2A FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TERT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5911 TETTH])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2b2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b2a OCA], [https://pdbe.org/2b2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b2a RCSB], [https://www.ebi.ac.uk/pdbsum/2b2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b2a ProSAT]</span></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=2b2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b2a OCA], [https://pdbe.org/2b2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b2a RCSB], [https://www.ebi.ac.uk/pdbsum/2b2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b2a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TERT_TETTH TERT_TETTH]] Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (By similarity).
| + | [https://www.uniprot.org/uniprot/TERT_TETTS TERT_TETTS] Catalytic component of telomerase, 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:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747).<ref>PMID:10944124</ref> <ref>PMID:15696174</ref> <ref>PMID:16462747</ref> <ref>PMID:17322903</ref> <ref>PMID:20713447</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Telomerase|Telomerase]] | |
| | *[[Telomerase 3D structures|Telomerase 3D structures]] | | *[[Telomerase 3D structures|Telomerase 3D structures]] |
| | *[[Telomerase Reverse Transcriptase|Telomerase Reverse Transcriptase]] | | *[[Telomerase Reverse Transcriptase|Telomerase Reverse Transcriptase]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA-directed DNA polymerase]] | + | [[Category: Tetrahymena thermophila]] |
| - | [[Category: Tetth]]
| + | [[Category: Cech TR]] |
| - | [[Category: Cech, T R]] | + | [[Category: Jacobs SA]] |
| - | [[Category: Jacobs, S A]] | + | [[Category: Podell ER]] |
| - | [[Category: Podell, E R]] | + | |
| - | [[Category: Reverse transcriptase]]
| + | |
| - | [[Category: Rt]]
| + | |
| - | [[Category: Telomerase]]
| + | |
| - | [[Category: Tert]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
TERT_TETTS Catalytic component of telomerase, 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:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747).[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Telomerase, a ribonucleoprotein enzyme, adds telomeric DNA repeats to the ends of linear chromosomes. Here we report the first high-resolution structure of any portion of the telomerase reverse transcriptase, the telomerase essential N-terminal (TEN) domain from Tetrahymena thermophila. The structure, which seems to represent a novel protein fold, shows phylogenetically conserved amino acid residues in a groove on its surface. These residues are crucial for telomerase catalytic activity, and several of them are required for sequence-specific binding of a single-stranded telomeric DNA primer. The positively charged C terminus, which becomes ordered upon interaction with other macromolecules, is involved in binding RNA in a non-sequence-specific manner. The TEN domain's ability to bind both RNA and telomeric DNA, coupled with the notably strong effects on activity upon mutagenesis of single surface residues, suggest how this domain contributes to telomerase catalysis.
Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase.,Jacobs SA, Podell ER, Cech TR Nat Struct Mol Biol. 2006 Mar;13(3):218-25. Epub 2006 Feb 5. PMID:16462747[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miller MC, Liu JK, Collins K. Template definition by Tetrahymena telomerase reverse transcriptase. EMBO J. 2000 Aug 15;19(16):4412-22. PMID:10944124 doi:10.1093/emboj/19.16.4412
- ↑ Prathapam R, Witkin KL, O'Connor CM, Collins K. A telomerase holoenzyme protein enhances telomerase RNA assembly with telomerase reverse transcriptase. Nat Struct Mol Biol. 2005 Mar;12(3):252-7. doi: 10.1038/nsmb900. Epub 2005 Feb 6. PMID:15696174 doi:http://dx.doi.org/10.1038/nsmb900
- ↑ Jacobs SA, Podell ER, Cech TR. Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase. Nat Struct Mol Biol. 2006 Mar;13(3):218-25. Epub 2006 Feb 5. PMID:16462747 doi:10.1038/nsmb1054
- ↑ Stone MD, Mihalusova M, O'connor CM, Prathapam R, Collins K, Zhuang X. Stepwise protein-mediated RNA folding directs assembly of telomerase ribonucleoprotein. Nature. 2007 Mar 22;446(7134):458-61. doi: 10.1038/nature05600. Epub 2007 Feb 25. PMID:17322903 doi:http://dx.doi.org/10.1038/nature05600
- ↑ Berman AJ, Gooding AR, Cech TR. Tetrahymena telomerase protein p65 induces conformational changes throughout telomerase RNA (TER) and rescues telomerase reverse transcriptase and TER assembly mutants. Mol Cell Biol. 2010 Oct;30(20):4965-76. doi: 10.1128/MCB.00827-10. Epub 2010 Aug , 16. PMID:20713447 doi:http://dx.doi.org/10.1128/MCB.00827-10
- ↑ Jacobs SA, Podell ER, Cech TR. Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase. Nat Struct Mol Biol. 2006 Mar;13(3):218-25. Epub 2006 Feb 5. PMID:16462747 doi:10.1038/nsmb1054
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