7QXB

Cryo-EM map of human telomerase-DNA-TPP1-POT1 complex (sharpened map)

7QXB の概要

• エントリーDOI: 10.2210/pdb7qxb/pdb
• 関連するPDBエントリー: 7QXA 7QXS
• EMDBエントリー: 14196 14197 14198 14199
• 分子名称: Telomerase reverse transcriptase, human telomerase RNA, Histone H2A, ... (7 entities in total)
• 機能のキーワード: reverse transcriptase, ribonucleoprotein, telomerase, telomere, dna binding protein, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 434924.07

構造登録者

Sekne, Z.,Ghanim, G.E.,van Roon, A.M.M.,Nguyen, T.H.D. (登録日: 2022-01-26, 公開日: 2022-03-02, 最終更新日: 2024-10-23)

主引用文献

Sekne, Z.,Ghanim, G.E.,van Roon, A.M.,Nguyen, T.H.D.
Structural basis of human telomerase recruitment by TPP1-POT1.
Science, 375:1173-1176, 2022

PubMed Abstract: Telomerase maintains genome stability by extending the 3' telomeric repeats at eukaryotic chromosome ends, thereby counterbalancing progressive loss caused by incomplete genome replication. In mammals, telomerase recruitment to telomeres is mediated by TPP1, which assembles as a heterodimer with POT1. We report structures of DNA-bound telomerase in complex with TPP1 and with TPP1-POT1 at 3.2- and 3.9-angstrom resolution, respectively. Our structures define interactions between telomerase and TPP1-POT1 that are crucial for telomerase recruitment to telomeres. The presence of TPP1-POT1 stabilizes the DNA, revealing an unexpected path by which DNA exits the telomerase active site and a DNA anchor site on telomerase that is important for telomerase processivity. Our findings rationalize extensive prior genetic and biochemical findings and provide a framework for future mechanistic work on telomerase regulation.

PubMed: 35201900
DOI: 10.1126/science.abn6840

実験手法

ELECTRON MICROSCOPY (3.9 Å)