4ABL

HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3

4ABL の概要

• エントリーDOI: 10.2210/pdb4abl/pdb
• 関連するPDBエントリー: 4ABK
• 分子名称: POLY [ADP-RIBOSE] POLYMERASE 14, BROMIDE ION (3 entities in total)
• 機能のキーワード: transferase, parp14
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: Q460N5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19888.46

構造登録者

Karlberg, T.,Moche, M.,Thorsell, A.G.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Ekblad, T.,Weigelt, J.,Schuler, H. (登録日: 2011-12-08, 公開日: 2012-12-19, 最終更新日: 2023-12-20)

主引用文献

Forst, A.H.,Karlberg, T.,Herzog, N.,Thorsell, A.G.,Gross, A.,Feijs, K.L.H.,Verheugd, P.,Kursula, P.,Nijmeijer, B.,Kremmer, E.,Kleine, H.,Ladurner, A.G.,Schuler, H.,Luscher, B.
Recognition of Mono-Adp-Ribosylated Artd10 Substrates by Artd8 Macrodomains
Structure, 21:462-, 2013

PubMed Abstract: ADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD(+) onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers that serve as adaptors for distinct protein domains. Other ARTs, exemplified by ARTD10, function as mono-ADP-ribosyltransferases, but it has been unclear whether this modification occurs in cells and how it is read. We observed that ARTD10 colocalized with ARTD8 and defined its macrodomains 2 and 3 as readers of mono-ADP-ribosylation both in vitro and in cells. The crystal structures of these two ARTD8 macrodomains and isothermal titration calorimetry confirmed their interaction with ADP-ribose. These macrodomains recognized mono-ADP-ribosylated ARTD10, but not poly-ADP-ribosylated ARTD1. This distinguished them from the macrodomain of macroH2A1.1, which interacted with poly- but not mono-ADP-ribosylated substrates. Moreover, Ran, an ARTD10 substrate, was also read by ARTD8 macrodomains. This identifies readers of mono-ADP-ribosylated proteins, defines their structures, and demonstrates the presence of this modification in cells.

PubMed: 23473667
DOI: 10.1016/J.STR.2012.12.019

実験手法

X-RAY DIFFRACTION (1.15 Å)