3V2B

Human poly(adp-ribose) polymerase 15 (ARTD7, BAL3), macro domain 2 in complex with adenosine-5-diphosphoribose

「3KH6」から置き換えられました

3V2B の概要

• エントリーDOI: 10.2210/pdb3v2b/pdb
• 分子名称: Poly [ADP-ribose] polymerase 15, [(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL [HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL] HYDROGEN PHOSPHATE (3 entities in total)
• 機能のキーワード: structural genomics, structural genomics consortium, sgc, poly (adp-ribose) polymerase, adp-ribose, bal3, b-aggressive lymphoma protein 3, glycosyltransferase, nucleus, transcription, transcription regulation, transferase, adp-ribosylation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (Probable): Q460N3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22149.92

構造登録者

Karlberg, T.,Moche, M.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, I.,Kallas, A.,Kotenyova, T.,Kotzcsh, A.,Kraulis, P.,Nielsen, T.K.,Nordlund, P.,Nyman, T.,Persson, C.,Roos, A.K.,Schutz, P.,Siponen, M.I.,Thorsell, A.G.,Tresaugues, L.,Van den berg, S.,Weigelt, J.,Welin, M.,Wisniewska, M.,Schuler, H.,Structural Genomics Consortium (SGC) (登録日: 2011-12-12, 公開日: 2011-12-21, 最終更新日: 2024-05-29)

主引用文献

Forst, A.H.,Karlberg, T.,Herzog, N.,Thorsell, A.G.,Gross, A.,Feijs, K.L.,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, 21:462-475, 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 (2.2 Å)