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< | ==Crystal structure of human poly(ADP-ribose) polymerase 15, catalytic fragment== | ||
<StructureSection load='3blj' size='340' side='right'caption='[[3blj]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3blj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BLJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BLJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=3blj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3blj OCA], [https://pdbe.org/3blj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3blj RCSB], [https://www.ebi.ac.uk/pdbsum/3blj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3blj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAR15_HUMAN PAR15_HUMAN] Transcriptional repressor. Has ADP-ribosyltransferase activity. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bl/3blj_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3blj ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The mammalian poly(ADP-ribose) polymerase (PARP) family are ADP-ribosyltransferases with diphtheria toxin homology (ARTD). Most members have mono-ADP-ribosyltransferase activity. PARP13/ARTD13, also called zinc finger antiviral protein (ZAP), has roles in viral immunity and microRNA mediated stress responses. PARP13 features a divergent PARP homology domain missing a PARP consensus sequence motif; the domain has enigmatic functions and apparently lacks catalytic activity. We used X-ray crystallography, molecular dynamics simulations and biochemical analyses to investigate the structural requirements for ADP-ribosyltransferase activity in human PARP13 and two of its functional partners in stress granules, PARP12/ARTD12, and PARP15/ BAL3/ARTD7. The crystal structure of the PARP homology domain of PARP13 shows obstruction of the canonical active site, precluding NAD+ binding. Molecular dynamics simulations indicate that this closed cleft conformation is maintained in solution. Introducing consensus side chains in PARP13 did not result in 3-aminobenzamide binding, but in further closure of the site. Three-dimensional alignment of the PARP homology domains of PARP13, PARP12, and PARP15 illustrates placement of PARP13 residues that deviate from the PARP family consensus. Introducing either one of two of these side chains into the corresponding positions in PARP15 abolished PARP15 ADP-ribosyltransferase activity. Taken together, our results show that PARP13 lacks the structural requirements for ADP-ribosyltransferase activity. | |||
Structural Basis for Lack of ADP-Ribosyltransferase Activity in Poly(ADP-Ribose) Polymerase-13/Zinc Finger Antiviral Protein.,Karlberg T, Klepsch M, Thorsell AG, Andersson CD, Linusson A, Schuler H J Biol Chem. 2015 Jan 29. pii: jbc.M114.630160. PMID:25635049<ref>PMID:25635049</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3blj" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Berglund H]] | |||
[[Category: Berglund | [[Category: Busam RD]] | ||
[[Category: Busam | [[Category: Collins R]] | ||
[[Category: Collins | [[Category: Dahlgren LG]] | ||
[[Category: Dahlgren | [[Category: Edwards AM]] | ||
[[Category: Edwards | [[Category: Flodin S]] | ||
[[Category: Flodin | [[Category: Flores A]] | ||
[[Category: Flores | [[Category: Graslund S]] | ||
[[Category: Graslund | [[Category: Hammarstrom M]] | ||
[[Category: Hammarstrom | [[Category: Johansson I]] | ||
[[Category: Johansson | [[Category: Kallas A]] | ||
[[Category: Kallas | [[Category: Karlberg T]] | ||
[[Category: Karlberg | [[Category: Kotenyova T]] | ||
[[Category: Kotenyova | [[Category: Lehtio L]] | ||
[[Category: Lehtio | [[Category: Moche M]] | ||
[[Category: Moche | [[Category: Nilsson ME]] | ||
[[Category: Nilsson | [[Category: Nordlund P]] | ||
[[Category: Nordlund | [[Category: Nyman T]] | ||
[[Category: Nyman | [[Category: Persson C]] | ||
[[Category: Persson | [[Category: Sagemark J]] | ||
[[Category: Svensson L]] | |||
[[Category: Sagemark | [[Category: Thorsell AG]] | ||
[[Category: Svensson | [[Category: Tresaugues L]] | ||
[[Category: Thorsell | [[Category: Van Den Berg S]] | ||
[[Category: Tresaugues | [[Category: Weigelt J]] | ||
[[Category: | [[Category: Welin M]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 15:10, 30 August 2023
Crystal structure of human poly(ADP-ribose) polymerase 15, catalytic fragmentCrystal structure of human poly(ADP-ribose) polymerase 15, catalytic fragment
Structural highlights
FunctionPAR15_HUMAN Transcriptional repressor. Has ADP-ribosyltransferase activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe mammalian poly(ADP-ribose) polymerase (PARP) family are ADP-ribosyltransferases with diphtheria toxin homology (ARTD). Most members have mono-ADP-ribosyltransferase activity. PARP13/ARTD13, also called zinc finger antiviral protein (ZAP), has roles in viral immunity and microRNA mediated stress responses. PARP13 features a divergent PARP homology domain missing a PARP consensus sequence motif; the domain has enigmatic functions and apparently lacks catalytic activity. We used X-ray crystallography, molecular dynamics simulations and biochemical analyses to investigate the structural requirements for ADP-ribosyltransferase activity in human PARP13 and two of its functional partners in stress granules, PARP12/ARTD12, and PARP15/ BAL3/ARTD7. The crystal structure of the PARP homology domain of PARP13 shows obstruction of the canonical active site, precluding NAD+ binding. Molecular dynamics simulations indicate that this closed cleft conformation is maintained in solution. Introducing consensus side chains in PARP13 did not result in 3-aminobenzamide binding, but in further closure of the site. Three-dimensional alignment of the PARP homology domains of PARP13, PARP12, and PARP15 illustrates placement of PARP13 residues that deviate from the PARP family consensus. Introducing either one of two of these side chains into the corresponding positions in PARP15 abolished PARP15 ADP-ribosyltransferase activity. Taken together, our results show that PARP13 lacks the structural requirements for ADP-ribosyltransferase activity. Structural Basis for Lack of ADP-Ribosyltransferase Activity in Poly(ADP-Ribose) Polymerase-13/Zinc Finger Antiviral Protein.,Karlberg T, Klepsch M, Thorsell AG, Andersson CD, Linusson A, Schuler H J Biol Chem. 2015 Jan 29. pii: jbc.M114.630160. PMID:25635049[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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