Summary information and primary citation
- PDB-id
- 3kyl; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- nucleic acid binding protein-DNA-RNA
- Method
- X-ray (2.7 Å)
- Summary
- Structure of the catalytic subunit of telomerase bound to its RNA template and telomeric DNA
- Reference
- Mitchell M, Gillis A, Futahashi M, Fujiwara H, Skordalakes E (2010): "Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA." Nat.Struct.Mol.Biol., 17, 513-518. doi: 10.1038/nsmb.1777.
- Abstract
- Telomerase is a specialized DNA polymerase that extends the 3' ends of eukaryotic linear chromosomes, a process required for genomic stability and cell viability. Here we present the crystal structure of the active Tribolium castaneum telomerase catalytic subunit, TERT, bound to an RNA-DNA hairpin designed to resemble the putative RNA-templating region and telomeric DNA. The RNA-DNA hybrid adopts a helical structure, docked in the interior cavity of the TERT ring. Contacts between the RNA template and motifs 2 and B' position the solvent-accessible RNA bases close to the enzyme active site for nucleotide binding and selectivity. Nucleic acid binding induces rigid TERT conformational changes to form a tight catalytic complex. Overall, TERT-RNA template and TERT-telomeric DNA associations are remarkably similar to those observed for retroviral reverse transcriptases, suggesting common mechanistic aspects of DNA replication between the two families of enzymes.
