4H4A

Crystal structure of the C-terminal domain of Drosophila melanogaster Zucchini

4H4A の概要

• エントリーDOI: 10.2210/pdb4h4a/pdb
• 分子名称: Mitochondrial cardiolipin hydrolase (2 entities in total)
• 機能のキーワード: phospholipase d fold, hkd motif, nuclease/phospholipid hydrolase, nucleic acid/phospholipid, hydrolase
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Mitochondrion outer membrane ; Single-pass membrane protein : Q9VKD7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19338.67

構造登録者

Voigt, F.,Schulz, E.C.,Barabas, O. (登録日: 2012-09-17, 公開日: 2012-11-07, 最終更新日: 2024-10-30)

主引用文献

Voigt, F.,Reuter, M.,Kasaruho, A.,Schulz, E.C.,Pillai, R.S.,Barabas, O.
Crystal structure of the primary piRNA biogenesis factor Zucchini reveals similarity to the bacterial PLD endonuclease Nuc.
Rna, 18:2128-2134, 2012

PubMed Abstract: Piwi-interacting RNAs (piRNAs) are a gonad-specific class of small RNAs that associate with the Piwi clade of Argonaute proteins and play a key role in transposon silencing in animals. Since biogenesis of piRNAs is independent of the double-stranded RNA-processing enzyme Dicer, an alternative nuclease that can process single-stranded RNA transcripts has been long sought. A Phospholipase D-like protein, Zucchini, that is essential for piRNA processing has been proposed to be a nuclease acting in piRNA biogenesis. Here we describe the crystal structure of Zucchini from Drosophila melanogaster and show that it is very similar to the bacterial endonuclease, Nuc. The structure also reveals that homodimerization induces major conformational changes assembling the active site. The active site is situated on the dimer interface at the bottom of a narrow groove that can likely accommodate single-stranded nucleic acid substrates. Furthermore, biophysical analysis identifies protein segments essential for dimerization and provides insights into regulation of Zucchini's activity.

PubMed: 23086923
DOI: 10.1261/rna.034967.112

実験手法

X-RAY DIFFRACTION (2.2 Å)