6D6V

CryoEM structure of Tetrahymena telomerase with telomeric DNA at 4.8 Angstrom resolution

これはPDB形式変換不可エントリーです。

6D6V の概要

• エントリーDOI: 10.2210/pdb6d6v/pdb
• EMDBエントリー: 7820 7821
• 分子名称: Telomerase-associated protein 82, Telomerase reverse transcriptase, Telomerase holoenzyme TEB heterotrimer Teb3 subunit, ... (9 entities in total)
• 機能のキーワード: telomerase, telomere, replication
• 由来する生物種: Tetrahymena thermophila; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 394987.00

構造登録者

Jiang, J.,Wang, Y.,Susac, L.,Chan, H.,Basu, R.,Zhou, Z.H.,Feigon, J. (登録日: 2018-04-22, 公開日: 2018-05-30, 最終更新日: 2025-07-16)

主引用文献

Jiang, J.,Wang, Y.,Susac, L.,Chan, H.,Basu, R.,Zhou, Z.H.,Feigon, J.
Structure of Telomerase with Telomeric DNA.
Cell, 173:1179-1190.e13, 2018

PubMed Abstract: Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA (TER). Its activity is a critical determinant of human health, affecting aging, cancer, and stem cell renewal. Lack of atomic models of telomerase, particularly one with DNA bound, has limited our mechanistic understanding of telomeric DNA repeat synthesis. We report the 4.8 Å resolution cryoelectron microscopy structure of active Tetrahymena telomerase bound to telomeric DNA. The catalytic core is an intricately interlocked structure of TERT and TER, including a previously structurally uncharacterized TERT domain that interacts with the TEN domain to physically enclose TER and regulate activity. This complete structure of a telomerase catalytic core and its interactions with telomeric DNA from the template to telomere-interacting p50-TEB complex provides unanticipated insights into telomerase assembly and catalytic cycle and a new paradigm for a reverse transcriptase RNP.

PubMed: 29775593
DOI: 10.1016/j.cell.2018.04.038

実験手法

ELECTRON MICROSCOPY (4.8 Å)