3V2B

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

Replaces:  3KH6

Summary for 3V2B

• Entry DOI: 10.2210/pdb3v2b/pdb
• Descriptor: 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)
• Functional Keywords: 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
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (Probable): Q460N3
• Total number of polymer chains: 1
• Total formula weight: 22149.92

Authors

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) (deposition date: 2011-12-12, release date: 2011-12-21, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)