3DU6

Structure of the catalytic subunit of telomerase, TERT

Summary for 3DU6

• Entry DOI: 10.2210/pdb3du6/pdb
• Related: 3DU5
• Descriptor: Telomerase reverse transcriptase (2 entities in total)
• Functional Keywords: reverse transcriptase, rna-directed dna polymerase, transferase
• Biological source: Tribolium castaneum (Red flour beetle)
• Total number of polymer chains: 2
• Total formula weight: 141177.44

Authors

Skordalakes, E. (deposition date: 2008-07-16, release date: 2008-08-26, Last modification date: 2024-02-21)

Primary citation

Gillis, A.J.,Schuller, A.P.,Skordalakes, E.
Structure of the Tribolium castaneum telomerase catalytic subunit TERT.
Nature, 455:633-637, 2008

PubMed Abstract: A common hallmark of human cancers is the overexpression of telomerase, a ribonucleoprotein complex that is responsible for maintaining the length and integrity of chromosome ends. Telomere length deregulation and telomerase activation is an early, and perhaps necessary, step in cancer cell evolution. Here we present the high-resolution structure of the Tribolium castaneum catalytic subunit of telomerase, TERT. The protein consists of three highly conserved domains, organized into a ring-like structure that shares common features with retroviral reverse transcriptases, viral RNA polymerases and B-family DNA polymerases. Domain organization places motifs implicated in substrate binding and catalysis in the interior of the ring, which can accommodate seven to eight bases of double-stranded nucleic acid. Modelling of an RNA-DNA heteroduplex in the interior of this ring demonstrates a perfect fit between the protein and the nucleic acid substrate, and positions the 3'-end of the DNA primer at the active site of the enzyme, providing evidence for the formation of an active telomerase elongation complex.

PubMed: 18758444
DOI: 10.1038/nature07283

Experimental method

X-RAY DIFFRACTION (2.71 Å)