5FIR

Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1

5FIR の概要

• エントリーDOI: 10.2210/pdb5fir/pdb
• 分子名称: 5'-3' EXORIBONUCLEASE 2 HOMOLOG, PAXT-1, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, 5'-3' exoribonuclease, mirna turnover
• 由来する生物種: CAENORHABDITIS ELEGANS; 詳細
• 細胞内の位置: Nucleus : Q9U299
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 505981.41

構造登録者

Richter, H.,Katic, I.,Gut, H.,Grosshans, H. (登録日: 2015-10-02, 公開日: 2016-01-20, 最終更新日: 2024-11-20)

主引用文献

Richter, H.,Katic, I.,Gut, H.,Grosshans, H.
Structural Basis and Function of Xrn2-Binding by Xtb Domains
Nat.Struct.Mol.Biol., 23:164-, 2016

PubMed Abstract: The RNase XRN2 is essential in RNA metabolism. In Caenorhabditis elegans, XRN2 functions with PAXT-1, which shares a putative XRN2-binding domain (XTBD) with otherwise unrelated mammalian proteins. Here, we characterize the structure and function of an XTBD-XRN2 complex. Although XTBD stably interconnects two XRN2 domains through numerous interacting residues, mutation of a single critical residue suffices to disrupt XTBD-XRN2 complexes in vitro and to recapitulate paxt-1-null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (HsC2AIL) can substitute for PAXT-1 in vivo. In vertebrates, which express three distinct XTBD-containing proteins, XRN2 may partition into distinct stable heterodimeric complexes, which probably differ in subcellular localization or function. In C. elegans, complex formation with PAXT-1, the sole XTBD protein, serves to preserve the stability of XRN2 in the absence of substrate.

PubMed: 26779609
DOI: 10.1038/NSMB.3155

実験手法

X-RAY DIFFRACTION (2.836 Å)