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{{STRUCTURE_3v2b|  PDB=3v2b  |  SCENE=  }}
==Human poly(adp-ribose) polymerase 15 (ARTD7, BAL3), macro domain 2 in complex with adenosine-5-diphosphoribose==
===Human poly(adp-ribose) polymerase 15 (ARTD7, BAL3), macro domain 2 in complex with adenosine-5-diphosphoribose===
<StructureSection load='3v2b' size='340' side='right' caption='[[3v2b]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3v2b]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V2B FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAL3, PARP15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v2b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v2b RCSB], [http://www.ebi.ac.uk/pdbsum/3v2b PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
[[3v2b]] is a 1 chain structure with sequence from [http://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].
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]]
*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]]
[[Category: Homo sapiens]]
== References ==
[[Category: Arrowsmith, C H.]]
<references/>
[[Category: Berglund, H.]]
__TOC__
[[Category: Bountra, C.]]
</StructureSection>
[[Category: Collins, R.]]
[[Category: Human]]
[[Category: Edwards, A M.]]
[[Category: Arrowsmith, C H]]
[[Category: Flodin, S.]]
[[Category: Berglund, H]]
[[Category: Flores, A.]]
[[Category: Bountra, C]]
[[Category: Graslund, S.]]
[[Category: Collins, R]]
[[Category: Hammarstrom, M.]]
[[Category: Edwards, A M]]
[[Category: Johansson, I.]]
[[Category: Flodin, S]]
[[Category: Kallas, A.]]
[[Category: Flores, A]]
[[Category: Karlberg, T.]]
[[Category: Graslund, S]]
[[Category: Kotenyova, T.]]
[[Category: Hammarstrom, M]]
[[Category: Kotzcsh, A.]]
[[Category: Johansson, I]]
[[Category: Kraulis, P.]]
[[Category: Kallas, A]]
[[Category: Moche, M.]]
[[Category: Karlberg, T]]
[[Category: Nielsen, T K.]]
[[Category: Kotenyova, T]]
[[Category: Nordlund, P.]]
[[Category: Kotzcsh, A]]
[[Category: Nyman, T.]]
[[Category: Kraulis, P]]
[[Category: Persson, C.]]
[[Category: Moche, M]]
[[Category: Roos, A K.]]
[[Category: Nielsen, T K]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Nordlund, P]]
[[Category: Schuler, H.]]
[[Category: Nyman, T]]
[[Category: Schutz, P.]]
[[Category: Persson, C]]
[[Category: Siponen, M I.]]
[[Category: Roos, A K]]
[[Category: Thorsell, A G.]]
[[Category: Structural genomic]]
[[Category: Tresaugues, L.]]
[[Category: Schuler, H]]
[[Category: Weigelt, J.]]
[[Category: Schutz, P]]
[[Category: Welin, M.]]
[[Category: Siponen, M I]]
[[Category: Wisniewska, M.]]
[[Category: Thorsell, A G]]
[[Category: Berg, S Van den.]]
[[Category: Tresaugues, L]]
[[Category: Weigelt, J]]
[[Category: Welin, M]]
[[Category: Wisniewska, M]]
[[Category: Berg, S Van den]]
[[Category: Adp-ribose]]
[[Category: Adp-ribose]]
[[Category: Adp-ribosylation]]
[[Category: Adp-ribosylation]]
Line 46: Line 62:
[[Category: Nucleus]]
[[Category: Nucleus]]
[[Category: Sgc]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Transcription]]
[[Category: Transcription]]
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 11:38, 18 December 2014

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

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:
Gene:BAL3, PARP15 (HUMAN)
Activity:NAD(+) ADP-ribosyltransferase, with EC number 2.4.2.30
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ 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. Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains. Structure. 2013 Mar 5;21(3):462-75. doi: 10.1016/j.str.2012.12.019. PMID:23473667 doi:http://dx.doi.org/10.1016/j.str.2012.12.019

3v2b, resolution 2.20Å

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