7W82

Crystal structure of maize RDR2

7W82 の概要

• エントリーDOI: 10.2210/pdb7w82/pdb
• 分子名称: RNA-dependent RNA polymerase (1 entity in total)
• 機能のキーワード: rdr2, rddm, rna polymerase, plant protein
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 115392.17

構造登録者

Du, X.,Yang, Z.,Du, J. (登録日: 2021-12-07, 公開日: 2022-06-08, 最終更新日: 2024-11-20)

主引用文献

Du, X.,Yang, Z.,Ariza, A.J.F.,Wang, Q.,Xie, G.,Li, S.,Du, J.
Structure of plant RNA-DEPENDENT RNA POLYMERASE 2, an enzyme involved in small interfering RNA production.
Plant Cell, 34:2140-2149, 2022

PubMed Abstract: In plants, the biogenesis of small interfering RNA (siRNA) requires a family of RNA-dependent RNA polymerases that convert single-stranded RNA (ssRNA) into double-stranded RNA (dsRNA), which is subsequently cleaved into defined lengths by Dicer endonucleases. Here, we determined the structure of maize (Zea mays) RNA-DEPENDENT RNA POLYMERASE 2 (ZmRDR2) in the closed and open conformations. The core catalytic region of ZmRDR2 possesses the canonical DNA-dependent RNA polymerase (DdRP) catalytic sites, pointing to a shared RNA production mechanism between DdRPs and plant RDR-family proteins. Apo-ZmRDR2 adopts a highly compact structure, representing an inactive closed conformation. By contrast, adding RNA induced a significant conformational change in the ZmRDR2 Head domain that opened the RNA binding tunnel, suggesting this is an active elongation conformation of ZmRDR2. Overall, our structural studies trapped both the active and inactive conformations of ZmRDR2, providing insights into the molecular mechanism of dsRNA synthesis during plant siRNA production.

PubMed: 35188193
DOI: 10.1093/plcell/koac067

実験手法

X-RAY DIFFRACTION (3.1 Å)