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5XXF

Crystal structure of Poz1, Tpz1 and Rap1

5XXF の概要
エントリーDOI10.2210/pdb5xxf/pdb
関連するPDBエントリー5XXE
分子名称Protection of telomeres protein poz1, Protection of telomeres protein tpz1, Rap1, ... (5 entities in total)
機能のキーワードtelomere, sheterin, hub, dna binding protein
由来する生物種Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
詳細
細胞内の位置Cytoplasm : O13852
Chromosome, telomere : O14246
タンパク質・核酸の鎖数6
化学式量合計70587.73
構造登録者
Xue, J.,Chen, H.,Wu, J.,Lei, M. (登録日: 2017-07-03, 公開日: 2017-12-20, 最終更新日: 2023-11-22)
主引用文献Xue, J.,Chen, H.,Wu, J.,Takeuchi, M.,Inoue, H.,Liu, Y.,Sun, H.,Chen, Y.,Kanoh, J.,Lei, M.
Structure of the fission yeast S. pombe telomeric Tpz1-Poz1-Rap1 complex.
Cell Res., 27:1503-1520, 2017
Cited by
PubMed Abstract: Telomeric shelterin complex caps chromosome ends and plays a crucial role in telomere maintenance and protection. In the fission yeast Schizosaccharomyces pombe, shelterin is composed of telomeric single- and double-stranded DNA-binding protein subcomplexes Pot1-Tpz1 and Taz1-Rap1, which are bridged by their interacting protein Poz1. However, the structure of Poz1 and how Poz1 functions as an interaction hub in the shelterin complex remain unclear. Here we report the crystal structure of Poz1 in complex with Poz1-binding motifs of Tpz1 and Rap1. The crystal structure shows that Poz1 employs two different binding surfaces to interact with Tpz1 and Rap1. Unexpectedly, the structure also reveals that Poz1 adopts a dimeric conformation. Mutational analyses suggest that proper interactions between Tpz1, Poz1, and Rap1 in the shelterin core complex are required for telomere length homeostasis and heterochromatin structure maintenance at telomeres. Structural resemblance between Poz1 and the TRFH domains of other shelterin proteins in fission yeast and humans suggests a model for the evolution of shelterin proteins.
PubMed: 29160296
DOI: 10.1038/cr.2017.145
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.1 Å)
構造検証レポート
Validation report summary of 5xxf
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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