2B2A

Crystal Structure of the TEN domain of the Telomerase Reverse Transcriptase

Summary for 2B2A

• Entry DOI: 10.2210/pdb2b2a/pdb
• Descriptor: Telomerase reverse transcriptase (2 entities in total)
• Functional Keywords: telomerase, tert, reverse transcriptase, rt, transferase
• Biological source: Tetrahymena thermophila
• Cellular location: Nucleus: O77448
• Total number of polymer chains: 3
• Total formula weight: 70865.45

Authors

Jacobs, S.A.,Podell, E.R.,Cech, T.R. (deposition date: 2005-09-18, release date: 2006-02-07, Last modification date: 2024-02-14)

Primary citation

Jacobs, S.A.,Podell, E.R.,Cech, T.R.
Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase.
Nat.Struct.Mol.Biol., 13:218-225, 2006

PubMed Abstract: 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.

PubMed: 16462747
DOI: 10.1038/nsmb1054

Experimental method

X-RAY DIFFRACTION (2.22 Å)