4Q8H

Structure of the Saccharomyces cerevisiae PAN2 pseudoubiquitin-hydrolase-RNase module

4Q8H の概要

• エントリーDOI: 10.2210/pdb4q8h/pdb
• 関連するPDBエントリー: 4Q8G 4Q8J
• 分子名称: PAB-dependent poly(A)-specific ribonuclease subunit PAN2, MAGNESIUM ION (2 entities in total)
• 機能のキーワード: ubiquitin carboxyl-terminal hydrolase-like domain, uch, rnase, pan3, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm: P53010
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76045.62

構造登録者

Schaefer, I.B.,Conti, E. (登録日: 2014-04-27, 公開日: 2014-06-04, 最終更新日: 2023-09-20)

主引用文献

Schafer, I.B.,Rode, M.,Bonneau, F.,Schussler, S.,Conti, E.
The structure of the Pan2-Pan3 core complex reveals cross-talk between deadenylase and pseudokinase.
Nat.Struct.Mol.Biol., 21:591-598, 2014

PubMed Abstract: Pan2-Pan3 is a conserved complex involved in the shortening of mRNA poly(A) tails, the initial step in eukaryotic mRNA turnover. We show that recombinant Saccharomyces cerevisiae Pan2-Pan3 can deadenylate RNAs in vitro without needing the poly(A)-binding protein Pab1. The crystal structure of an active ~200-kDa core complex reveals that Pan2 and Pan3 interact with an unusual 1:2 stoichiometry imparted by the asymmetric nature of the Pan3 homodimer. An extended region of Pan2 wraps around Pan3 and provides a major anchoring point for complex assembly. A Pan2 module formed by the pseudoubiquitin-hydrolase and RNase domains latches onto the Pan3 pseudokinase with intertwined interactions that orient the deadenylase active site toward the A-binding site of the interacting Pan3. The molecular architecture of Pan2-Pan3 suggests how the nuclease and its pseudokinase regulator act in synergy to promote deadenylation.

PubMed: 24880344
DOI: 10.1038/nsmb.2834

実験手法

X-RAY DIFFRACTION (3.1 Å)