5AF0

MAEL domain from Bombyx mori Maelstrom

5AF0 の概要

• エントリーDOI: 10.2210/pdb5af0/pdb
• 分子名称: MAELSTROM, ZINC ION (3 entities in total)
• 機能のキーワード: unknown protein, mael, pirna, ribonuclease, fusion protein, piwi
• 由来する生物種: BOMBYX MORI (SILK MOTH); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119657.54

構造登録者

Chen, K.,Campbell, E.,Pandey, R.R.,Yang, Z.,McCarthy, A.A.,Pillai, R.S. (登録日: 2015-01-13, 公開日: 2015-04-01, 最終更新日: 2024-05-08)

主引用文献

Chen, K.,Campbell, E.,Pandey, R.R.,Yang, Z.,Mccarthy, A.A.,Pillai, R.S.
Metazoan Maelstrom is an RNA-Binding Protein that Has Evolved from an Ancient Nuclease Active in Protists.
RNA, 21:833-, 2015

PubMed Abstract: Piwi-interacting RNAs (piRNAs) guide Piwi argonautes to their transposon targets for silencing. The highly conserved protein Maelstrom is linked to both piRNA biogenesis and effector roles in this pathway. One defining feature of Maelstrom is the predicted MAEL domain of unknown molecular function. Here, we present the first crystal structure of the MAEL domain from Bombyx Maelstrom, which reveals a nuclease fold. The overall architecture resembles that found in Mg(2+)- or Mn(2+)-dependent DEDD nucleases, but a clear distinguishing feature is the presence of a structural Zn(2+) ion coordinated by the conserved ECHC residues. Strikingly, metazoan Maelstrom orthologs across the animal kingdom lack the catalytic DEDD residues, and as we show for Bombyx Maelstrom are inactive as nucleases. However, a MAEL domain-containing protein from amoeba having both sequence motifs (DEDD and ECHC) is robustly active as an exoribonuclease. Finally, we show that the MAEL domain of Bombyx Maelstrom displays a strong affinity for single-stranded RNAs. Our studies suggest that the ancient MAEL nuclease domain evolved to function as an RNA-binding module in metazoan Maelstrom.

PubMed: 25778731
DOI: 10.1261/RNA.049437.114

実験手法

X-RAY DIFFRACTION (2.401 Å)