7U5C

Cryo-EM structure of human CST bound to DNA polymerase alpha-primase in a recruitment state

7U5C の概要

• エントリーDOI: 10.2210/pdb7u5c/pdb
• EMDBエントリー: 26346
• 分子名称: DNA primase small subunit, IRON/SULFUR CLUSTER, DNA primase large subunit, ... (10 entities in total)
• 機能のキーワード: fill-in, telomere, replication, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 502115.02

構造登録者

Cai, S.W.,Zinder, J.C.,Svetlov, V.,Bush, M.W.,Nudler, E.,Walz, T.,de Lange, T. (登録日: 2022-03-02, 公開日: 2022-05-18, 最終更新日: 2024-02-14)

主引用文献

Cai, S.W.,Zinder, J.C.,Svetlov, V.,Bush, M.W.,Nudler, E.,Walz, T.,de Lange, T.
Cryo-EM structure of the human CST-Pol alpha /primase complex in a recruitment state.
Nat.Struct.Mol.Biol., 29:813-819, 2022

PubMed Abstract: The CST-Polα/primase complex is essential for telomere maintenance and functions to counteract resection at double-strand breaks. We report a 4.6-Å resolution cryo-EM structure of human CST-Polα/primase, captured prior to catalysis in a recruitment state stabilized by chemical cross-linking. Our structure reveals an evolutionarily conserved interaction between the C-terminal domain of the catalytic POLA1 subunit and an N-terminal expansion in metazoan CTC1. Cross-linking mass spectrometry and negative-stain EM analysis provide insight into CST binding by the flexible POLA1 N-terminus. Finally, Coats plus syndrome disease mutations previously characterized to disrupt formation of the CST-Polα/primase complex map to protein-protein interfaces observed in the recruitment state. Together, our results shed light on the architecture and stoichiometry of the metazoan fill-in machinery.

PubMed: 35578024
DOI: 10.1038/s41594-022-00766-y

実験手法

ELECTRON MICROSCOPY (4.6 Å)