3v2b

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

spinqualitylabelsall models 3v2b, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v2b is a 1 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 3kh6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AR6 Gene: BAL3, PARP15 (HUMAN) Activity: NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAR15_HUMAN] Transcriptional repressor. Has ADP-ribosyltransferase activity. Publication Abstract from PubMed 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. Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains.,Forst AH, Karlberg T, Herzog N, Thorsell AG, Gross A, Feijs KL, Verheugd P, Kursula P, Nijmeijer B, Kremmer E, Kleine H, Ladurner AG, Schuler H, Luscher B Structure. 2013 Mar 5;21(3):462-75. doi: 10.1016/j.str.2012.12.019. PMID:23473667 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Poly (ADP-ribose) polymerase

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