4ABK
HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3 IN COMPLEX WITH ADENOSINE- 5-DIPHOSPHORIBOSE
Summary for 4ABK
Entry DOI | 10.2210/pdb4abk/pdb |
Related | 4ABL |
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 | transferase, parp14, artd8 |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Nucleus: Q460N5 |
Total number of polymer chains | 1 |
Total formula weight | 20367.87 |
Authors | Karlberg, T.,Moche, M.,Thorsell, A.G.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Ekblad, T.,Weigelt, J.,Schuler, H. (deposition date: 2011-12-08, release date: 2012-12-19, Last modification date: 2023-12-20) |
Primary citation | 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 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 (1.6 Å) |
Structure validation
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