3v2b

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<StructureSection load='3v2b' size='340' side='right'caption='[[3v2b]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3v2b' size='340' side='right'caption='[[3v2b]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kh6 3kh6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V2B FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kh6 3kh6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V2B FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AR6:[(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'>AR6</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAL3, PARP15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AR6:[(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'>AR6</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2b OCA], [https://pdbe.org/3v2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v2b RCSB], [https://www.ebi.ac.uk/pdbsum/3v2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v2b ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2b OCA], [https://pdbe.org/3v2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v2b RCSB], [https://www.ebi.ac.uk/pdbsum/3v2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v2b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PAR15_HUMAN PAR15_HUMAN]] Transcriptional repressor. Has ADP-ribosyltransferase activity.
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[https://www.uniprot.org/uniprot/PAR15_HUMAN PAR15_HUMAN] Transcriptional repressor. Has ADP-ribosyltransferase activity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:23473667</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3v2b" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Berglund, H]]
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[[Category: Berglund H]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Collins, R]]
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[[Category: Collins R]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Flodin, S]]
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[[Category: Flodin S]]
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[[Category: Flores, A]]
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[[Category: Flores A]]
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[[Category: Graslund, S]]
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[[Category: Graslund S]]
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[[Category: Hammarstrom, M]]
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[[Category: Hammarstrom M]]
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[[Category: Johansson, I]]
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[[Category: Johansson I]]
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[[Category: Kallas, A]]
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[[Category: Kallas A]]
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[[Category: Karlberg, T]]
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[[Category: Karlberg T]]
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[[Category: Kotenyova, T]]
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[[Category: Kotenyova T]]
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[[Category: Kotzcsh, A]]
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[[Category: Kotzcsh A]]
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[[Category: Kraulis, P]]
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[[Category: Kraulis P]]
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[[Category: Moche, M]]
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[[Category: Moche M]]
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[[Category: Nielsen, T K]]
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[[Category: Nielsen TK]]
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[[Category: Nordlund, P]]
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[[Category: Nordlund P]]
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[[Category: Nyman, T]]
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[[Category: Nyman T]]
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[[Category: Persson, C]]
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[[Category: Persson C]]
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[[Category: Roos, A K]]
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[[Category: Roos AK]]
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[[Category: Structural genomic]]
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[[Category: Schuler H]]
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[[Category: Schuler, H]]
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[[Category: Schutz P]]
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[[Category: Schutz, P]]
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[[Category: Siponen MI]]
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[[Category: Siponen, M I]]
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[[Category: Thorsell AG]]
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[[Category: Thorsell, A G]]
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[[Category: Tresaugues L]]
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[[Category: Tresaugues, L]]
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[[Category: Van den berg S]]
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[[Category: Weigelt, J]]
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[[Category: Weigelt J]]
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[[Category: Welin, M]]
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[[Category: Welin M]]
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[[Category: Wisniewska, M]]
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[[Category: Wisniewska M]]
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[[Category: Berg, S Van den]]
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[[Category: Adp-ribose]]
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[[Category: Adp-ribosylation]]
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[[Category: B-aggressive lymphoma protein 3]]
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[[Category: Bal3]]
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[[Category: Glycosyltransferase]]
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[[Category: Nucleus]]
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[[Category: Sgc]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transferase]]
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Revision as of 14:15, 14 March 2024

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

PDB ID 3v2b

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OCA

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