7SZ3

Mouse PARP13/ZAP ZnF5-WWE1-WWE2 bound to ADPr

7SZ3 の概要

• エントリーDOI: 10.2210/pdb7sz3/pdb
• 分子名称: Zinc finger CCCH-type antiviral protein 1, GLYCEROL, ADENOSINE-5-DIPHOSPHORIBOSE, ... (5 entities in total)
• 機能のキーワード: parp13, zap, wwe, adpr, poly-adpribose, antiviral protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49383.29

構造登録者

Ayanath Kuttiyatveetil, J.R.,Pascal, J.M. (登録日: 2021-11-25, 公開日: 2022-10-05, 最終更新日: 2024-05-22)

主引用文献

Kuttiyatveetil, J.R.A.,Soufari, H.,Dasovich, M.,Uribe, I.R.,Mirhasan, M.,Cheng, S.J.,Leung, A.K.L.,Pascal, J.M.
Crystal structures and functional analysis of the ZnF5-WWE1-WWE2 region of PARP13/ZAP define a distinctive mode of engaging poly(ADP-ribose).
Cell Rep, 41:111529-111529, 2022

PubMed Abstract: PARP13/ZAP (zinc-finger antiviral protein) acts against multiple viruses by promoting degradation of viral mRNA. PARP13 has four N-terminal zinc (Zn) fingers that bind CG-rich nucleotide sequences, a C-terminal ADP ribosyltransferase fold, and a central region with a fifth Zn finger and tandem WWE domains. The central PARP13 region, ZnF5-WWE1-WWE2, is implicated in binding poly(ADP-ribose); however, there are limited insights into its structure and function. We present crystal structures of ZnF5-WWE1-WWE2 from mouse PARP13 in complex with ADP-ribose and in complex with ATP. The crystal structures and binding studies demonstrate that WWE2 interacts with ADP-ribose and ATP, whereas WWE1 does not have a functional binding site. Binding studies with poly(ADP-ribose) ligands indicate that WWE2 serves as an anchor for preferential binding to the terminal end of poly(ADP-ribose) chains. The composite ZnF5-WWE1-WWE2 structure forms an extended surface to engage ADP-ribose chains, representing a distinctive mode of recognition that provides a framework for investigating the impact of poly(ADP-ribose) on PARP13 function.

PubMed: 36288691
DOI: 10.1016/j.celrep.2022.111529

実験手法

X-RAY DIFFRACTION (2.2 Å)