3Q71
Human parp14 (artd8) - macro domain 2 in complex with adenosine-5-diphosphoribose
Summary for 3Q71
| Entry DOI | 10.2210/pdb3q71/pdb |
| Descriptor | Poly [ADP-ribose] polymerase 14, [(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, transferase, parp14 macro 2 |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus : Q460N5 |
| Total number of polymer chains | 1 |
| Total formula weight | 24896.01 |
| Authors | Karlberg, T.,Siponen, M.I.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Ekblad, T.,Flodin, S.,Flores, A.,Graslund, S.,Kotenyova, T.,Kouznetsova, E.,Moche, M.,Nordlund, P.,Nyman, T.,Persson, C.,Sehic, A.,Thorsell, A.G.,Tresaugues, L.,Wahlberg, E.,Weigelt, J.,Welin, M.,Schuler, H.,Structural Genomics Consortium (SGC) (deposition date: 2011-01-04, release date: 2011-01-26, Last modification date: 2023-09-13) |
| 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 Cited by 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: 23473667DOI: 10.1016/j.str.2012.12.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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