2B2A

Crystal Structure of the TEN domain of the Telomerase Reverse Transcriptase

2B2A の概要

• エントリーDOI: 10.2210/pdb2b2a/pdb
• 分子名称: Telomerase reverse transcriptase (2 entities in total)
• 機能のキーワード: telomerase, tert, reverse transcriptase, rt, transferase
• 由来する生物種: Tetrahymena thermophila
• 細胞内の位置: Nucleus: O77448
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 70865.45

構造登録者

Jacobs, S.A.,Podell, E.R.,Cech, T.R. (登録日: 2005-09-18, 公開日: 2006-02-07, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.22 Å)