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4iqy

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Revision as of 21:05, 16 November 2022

Crystal structure of the human protein-proximal ADP-ribosyl-hydrolase MacroD2

Structural highlights

4iqy is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MACD2_HUMAN Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.^[1]

Publication Abstract from PubMed

ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD(+) to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid substrates, often in response to DNA damage or other stresses. Poly-ADPr-glycohydrolase readily reverses poly-ADP-ribosylation induced by the DNA-damage sensor PARP1 and other enzymes, but it does not remove the most proximal ADPr linked to the target amino acid. Searches for enzymes capable of fully reversing cellular mono-ADP-ribosylation back to the unmodified state have proved elusive, which leaves a gap in the understanding of this modification. Here, we identify a family of macrodomain enzymes present in viruses, yeast and animals that reverse cellular ADP-ribosylation by acting on mono-ADP-ribosylated substrates. Our discoveries establish the complete reversibility of PARP-catalyzed cellular ADP-ribosylation as a regulatory modification.

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation.,Jankevicius G, Hassler M, Golia B, Rybin V, Zacharias M, Timinszky G, Ladurner AG Nat Struct Mol Biol. 2013 Apr;20(4):508-14. doi: 10.1038/nsmb.2523. Epub 2013 Mar, 10. PMID:23474712^[2]

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

References

↑ Chen D, Vollmar M, Rossi MN, Phillips C, Kraehenbuehl R, Slade D, Mehrotra PV, von Delft F, Crosthwaite SK, Gileadi O, Denu JM, Ahel I. Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. J Biol Chem. 2011 Apr 15;286(15):13261-71. Epub 2011 Jan 21. PMID:21257746 doi:10.1074/jbc.M110.206771
↑ Jankevicius G, Hassler M, Golia B, Rybin V, Zacharias M, Timinszky G, Ladurner AG. A family of macrodomain proteins reverses cellular mono-ADP-ribosylation. Nat Struct Mol Biol. 2013 Apr;20(4):508-14. doi: 10.1038/nsmb.2523. Epub 2013 Mar, 10. PMID:23474712 doi:http://dx.doi.org/10.1038/nsmb.2523

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4iqy"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the human protein-proximal ADP-ribosyl-hydrolase MacroD2==
-<StructureSection load='4iqy' size='340' side='right' caption='[[4iqy]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
+<StructureSection load='4iqy' size='340' side='right'caption='[[4iqy]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4iqy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IQY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4iqy]] 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=4IQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IQY 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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MACROD2, C20orf133 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iqy OCA], [https://pdbe.org/4iqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iqy RCSB], [https://www.ebi.ac.uk/pdbsum/4iqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iqy ProSAT]</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=4iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iqy OCA], [http://pdbe.org/4iqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iqy RCSB], [http://www.ebi.ac.uk/pdbsum/4iqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iqy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MACD2_HUMAN MACD2_HUMAN]] Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.<ref>PMID:21257746</ref>
+[https://www.uniprot.org/uniprot/MACD2_HUMAN MACD2_HUMAN] Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.<ref>PMID:21257746</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Golia, B]]
+[[Category: Large Structures]]
-[[Category: Hassler, M]]
+[[Category: Golia B]]
-[[Category: Jankevicius, G]]
+[[Category: Hassler M]]
-[[Category: Ladurner, A G]]
+[[Category: Jankevicius G]]
-[[Category: Rybin, V]]
+[[Category: Ladurner AG]]
-[[Category: Timinszky, G]]
+[[Category: Rybin V]]
-[[Category: Zacharias, M]]
+[[Category: Timinszky G]]
-[[Category: Adp-ribose binding]]
+[[Category: Zacharias M]]
-[[Category: Adp-ribosylation]]
-[[Category: Hydrolase]]
-[[Category: Macrodomain]]
-[[Category: Nuclear/cytoplasmic]]

4iqy

From Proteopedia

Revision as of 21:05, 16 November 2022

Crystal structure of the human protein-proximal ADP-ribosyl-hydrolase MacroD2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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