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Crystal Structure of the TEN domain of the Telomerase Reverse TranscriptaseCrystal Structure of the TEN domain of the Telomerase Reverse Transcriptase
Structural highlights
Function[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). Publication Abstract from PubMedTelomerase, 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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