3VFQ

Human PARP14 (ARTD8, BAL2) - macro domains 1 and 2 in complex with adenosine-5-diphosphoribose

Summary for 3VFQ

• Entry DOI: 10.2210/pdb3vfq/pdb
• Related: 4D86
• 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 (2 entities in total)
• Functional Keywords: transferase, adp-ribose, parp14, macro, bal2, artd8, structural genomics, structural genomics consortium, sgc
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q460N5
• Total number of polymer chains: 1
• Total formula weight: 45266.73

Authors

Karlberg, T.,Thorsell, A.G.,Arrowsmith, C.H.,Bountra, C.,Edwards, A.M.,Ekblad, T.,Weigelt, J.,Schuler, H.,Structural Genomics Consortium (SGC) (deposition date: 2012-01-10, release date: 2013-03-13, 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

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 (2.8 Å)