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6LBS

Crystal structure of yeast Stn1

6LBS の概要
エントリーDOI10.2210/pdb6lbs/pdb
関連するPDBエントリー6LBR
分子名称KLLA0C11825p (2 entities in total)
機能のキーワードtelomere, cst complex, dna binding protein
由来する生物種Kluyveromyces lactis (Yeast)
タンパク質・核酸の鎖数6
化学式量合計117763.90
構造登録者
Ge, Y.,Wu, Z.,Wu, J.,Lei, M. (登録日: 2019-11-14, 公開日: 2020-07-15, 最終更新日: 2024-10-16)
主引用文献Ge, Y.,Wu, Z.,Chen, H.,Zhong, Q.,Shi, S.,Li, G.,Wu, J.,Lei, M.
Structural insights into telomere protection and homeostasis regulation by yeast CST complex.
Nat.Struct.Mol.Biol., 27:752-762, 2020
Cited by
PubMed Abstract: Budding yeast Cdc13-Stn1-Ten1 (CST) complex plays an essential role in telomere protection and maintenance. Despite extensive studies, only structural information of individual domains of CST is available; the architecture of CST still remains unclear. Here, we report crystal structures of Kluyveromyces lactis Cdc13-telomeric-DNA, Cdc13-Stn1 and Stn1-Ten1 complexes and propose an integrated model depicting how CST assembles and plays its roles at telomeres. Surprisingly, two oligonucleotide/oligosaccharide-binding (OB) folds of Cdc13 (OB2 and OB4), previously believed to mediate Cdc13 homodimerization, actually form a stable intramolecular interaction. This OB2-OB4 module of Cdc13 is required for the Cdc13-Stn1 interaction that assembles CST into an architecture with a central ring-like core and multiple peripheral modules in a 2:2:2 stoichiometry. Functional analyses indicate that this unique CST architecture is essential for both telomere capping and homeostasis regulation. Overall, our results provide fundamentally valuable structural information regarding the CST complex and its roles in telomere biology.
PubMed: 32661422
DOI: 10.1038/s41594-020-0459-8
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 6lbs
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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