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4ABK

HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3 IN COMPLEX WITH ADENOSINE- 5-DIPHOSPHORIBOSE

Summary for 4ABK
Entry DOI10.2210/pdb4abk/pdb
Related4ABL
DescriptorPOLY [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 Keywordstransferase, parp14, artd8
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationNucleus: Q460N5
Total number of polymer chains1
Total formula weight20367.87
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 citationForst, 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: 23473667
DOI: 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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