3KYL

Structure of the catalytic subunit of telomerase bound to its RNA template and telomeric DNA

Summary for 3KYL

• Entry DOI: 10.2210/pdb3kyl/pdb
• Descriptor: Telomerase reverse transcriptase, DNA/RNA (5'-R(*CP*UP*GP*AP*CP*CP*UP*GP*AP*C)-D(P*TP*TP*CP*GP*GP*TP*CP*AP*GP*GP*TP*CP*AP*G)-3'), MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: reverse transcriptase, protein-rna-dna complex, telomerase, rna-directed dna polymerase, nucleic acid binding protein-dna-rna complex, nucleic acid binding protein/dna/rna
• Biological source: Tribolium castaneum (rust-red flour beetle)
• Total number of polymer chains: 2
• Total formula weight: 78106.71

Authors

Skordalakes, E. (deposition date: 2009-12-06, release date: 2010-03-31, Last modification date: 2024-02-21)

Primary citation

Mitchell, M.,Gillis, A.,Futahashi, M.,Fujiwara, H.,Skordalakes, E.
Structural basis for telomerase catalytic subunit TERT binding to RNA template and telomeric DNA.
Nat.Struct.Mol.Biol., 17:513-518, 2010

PubMed 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.

PubMed: 20357774
DOI: 10.1038/nsmb.1777

Experimental method

X-RAY DIFFRACTION (2.7 Å)