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7O6N

Crystal structure of C. elegans ERH-2 PID-3 complex

7O6N の概要
エントリーDOI10.2210/pdb7o6n/pdb
関連するPDBエントリー7O6L
分子名称Enhancer of rudimentary homolog 2, Protein pid-3, FORMIC ACID, ... (4 entities in total)
機能のキーワードerh-2 pid-3 complex pirna processing petisco, protein binding
由来する生物種Caenorhabditis elegans
詳細
タンパク質・核酸の鎖数4
化学式量合計32706.51
構造登録者
Falk, S.,Ketting, R.F. (登録日: 2021-04-11, 公開日: 2021-08-25, 最終更新日: 2024-01-31)
主引用文献Perez-Borrajero, C.,Podvalnaya, N.,Holleis, K.,Lichtenberger, R.,Karaulanov, E.,Simon, B.,Basquin, J.,Hennig, J.,Ketting, R.F.,Falk, S.
Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans .
Genes Dev., 35:1304-1323, 2021
Cited by
PubMed Abstract: Piwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5' and 3' processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We used biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: PID-1 governs 21U processing, whereas TOST-1 links PETISCO to an unknown process essential for early embryogenesis. Here, we show that PETISCO forms an octameric assembly with each subunit present in two copies. Determination of structures of the TOFU-6/PID-3 and PID-3/ERH-2 subcomplexes, supported by in vivo studies of subunit interaction mutants, allows us to propose a model for the formation of the TOFU-6/PID-3/ERH-2 core complex and its functionality in germ cells and early embryos. Using NMR spectroscopy, we demonstrate that TOST-1 and PID-1 bind to a common surface on ERH-2, located opposite its PID-3 binding site, explaining how PETISCO can mediate different cellular roles.
PubMed: 34413138
DOI: 10.1101/gad.348648.121
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.17 Å)
構造検証レポート
Validation report summary of 7o6n
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2026-04-22に公開中

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