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6F3H

Crystal structure of Dss1 exoribonuclease active site mutant D477N from Candida glabrata

6F3H の概要
エントリーDOI10.2210/pdb6f3h/pdb
分子名称Exoribonuclease II, mitochondrial, RNA (5'-R(P*AP*GP*AP*UP*AP*C)-3'), RNA (5'-R(P*CP*AP*CP*UP*GP*A)-3'), ... (5 entities in total)
機能のキーワード3' to 5' exoribonuclease rna degradation mitochondria, hydrolase
由来する生物種Candida glabrata (Yeast)
詳細
タンパク質・核酸の鎖数4
化学式量合計194510.50
構造登録者
Razew, M.,Nowak, E.,Nowotny, M. (登録日: 2017-11-28, 公開日: 2018-01-17, 最終更新日: 2024-11-20)
主引用文献Razew, M.,Warkocki, Z.,Taube, M.,Kolondra, A.,Czarnocki-Cieciura, M.,Nowak, E.,Labedzka-Dmoch, K.,Kawinska, A.,Piatkowski, J.,Golik, P.,Kozak, M.,Dziembowski, A.,Nowotny, M.
Structural analysis of mtEXO mitochondrial RNA degradosome reveals tight coupling of nuclease and helicase components.
Nat Commun, 9:97-97, 2018
Cited by
PubMed Abstract: Nuclease and helicase activities play pivotal roles in various aspects of RNA processing and degradation. These two activities are often present in multi-subunit complexes from nucleic acid metabolism. In the mitochondrial exoribonuclease complex (mtEXO) both enzymatic activities are tightly coupled making it an excellent minimal system to study helicase-exoribonuclease coordination. mtEXO is composed of Dss1 3'-to-5' exoribonuclease and Suv3 helicase. It is the master regulator of mitochondrial gene expression in yeast. Here, we present the structure of mtEXO and a description of its mechanism of action. The crystal structure of Dss1 reveals domains that are responsible for interactions with Suv3. Importantly, these interactions are compatible with the conformational changes of Suv3 domains during the helicase cycle. We demonstrate that mtEXO is an intimate complex which forms an RNA-binding channel spanning its entire structure, with Suv3 helicase feeding the 3' end of the RNA toward the active site of Dss1.
PubMed: 29311576
DOI: 10.1038/s41467-017-02570-5
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.703 Å)
構造検証レポート
Validation report summary of 6f3h
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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