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==Human Poly(ADP-Ribose) Polymerase 12, Catalytic fragment in complex with an inhibitor 3-Aminobenzoic acid== | ==Human Poly(ADP-Ribose) Polymerase 12, Catalytic fragment in complex with an inhibitor 3-Aminobenzoic acid== | ||
<StructureSection load='2pqf' size='340' side='right' caption='[[2pqf]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2pqf' size='340' side='right'caption='[[2pqf]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pqf]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2pqf]] is a 6 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=2PQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQF FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GAB:3-AMINOBENZOIC+ACID'>GAB</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2pqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pqf OCA], [https://pdbe.org/2pqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pqf RCSB], [https://www.ebi.ac.uk/pdbsum/2pqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pqf ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PAR12_HUMAN PAR12_HUMAN] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pqf_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pqf_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=2pqf ConSurf]. | ||
<div style="clear:both"></div> | <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 2pqf" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]] | *[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: Berglund | [[Category: Berglund H]] | ||
[[Category: Busam | [[Category: Busam RD]] | ||
[[Category: Collins | [[Category: Collins R]] | ||
[[Category: Dahlgren | [[Category: Dahlgren LG]] | ||
[[Category: Edwards | [[Category: Edwards A]] | ||
[[Category: Flodin | [[Category: Flodin S]] | ||
[[Category: Flores | [[Category: Flores A]] | ||
[[Category: Graslund | [[Category: Graslund S]] | ||
[[Category: Hammarstrom | [[Category: Hammarstrom M]] | ||
[[Category: Hogbom | [[Category: Hogbom M]] | ||
[[Category: Holmberg-Schiavone | [[Category: Holmberg-Schiavone L]] | ||
[[Category: Johansson | [[Category: Johansson I]] | ||
[[Category: Kallas | [[Category: Kallas A]] | ||
[[Category: Karlberg | [[Category: Karlberg T]] | ||
[[Category: Kotenyova | [[Category: Kotenyova T]] | ||
[[Category: Lehtio | [[Category: Lehtio L]] | ||
[[Category: Moche | [[Category: Moche M]] | ||
[[Category: Nordlund | [[Category: Nordlund P]] | ||
[[Category: Nyman | [[Category: Nyman T]] | ||
[[Category: Persson | [[Category: Persson C]] | ||
[[Category: Sagemark J]] | |||
[[Category: Sagemark | [[Category: Sundstrom M]] | ||
[[Category: Sundstrom | [[Category: Thorsell AG]] | ||
[[Category: Thorsell | [[Category: Van Den Berg S]] | ||
[[Category: | [[Category: Weigelt J]] | ||
[[Category: | |||
Latest revision as of 08:26, 17 October 2024
Human Poly(ADP-Ribose) Polymerase 12, Catalytic fragment in complex with an inhibitor 3-Aminobenzoic acidHuman Poly(ADP-Ribose) Polymerase 12, Catalytic fragment in complex with an inhibitor 3-Aminobenzoic acid
Structural highlights
FunctionEvolutionary 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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