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| | <StructureSection load='2bfr' size='340' side='right'caption='[[2bfr]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2bfr' size='340' side='right'caption='[[2bfr]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hjz|1hjz]], [[1vhu|1vhu]], [[2bfq|2bfq]]</div></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=2bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfr OCA], [https://pdbe.org/2bfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfr RCSB], [https://www.ebi.ac.uk/pdbsum/2bfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfr 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=2bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfr OCA], [https://pdbe.org/2bfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfr RCSB], [https://www.ebi.ac.uk/pdbsum/2bfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Y1521_ARCFU Y1521_ARCFU]] Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency.<ref>PMID:23474712</ref> <ref>PMID:15902274</ref>
| + | [https://www.uniprot.org/uniprot/Y1521_ARCFU Y1521_ARCFU] Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency.<ref>PMID:23474712</ref> <ref>PMID:15902274</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arcfl]] | + | [[Category: Archaeoglobus fulgidus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allen, M D]] | + | [[Category: Allen MD]] |
| - | [[Category: Buhecha, H R]] | + | [[Category: Buhecha HR]] |
| - | [[Category: Bycroft, M]] | + | [[Category: Bycroft M]] |
| - | [[Category: Karras, G I]] | + | [[Category: Karras GI]] |
| - | [[Category: Ladurner, A G]] | + | [[Category: Ladurner AG]] |
| - | [[Category: Pugieux, C]] | + | [[Category: Pugieux C]] |
| - | [[Category: Sait, F]] | + | [[Category: Sait F]] |
| - | [[Category: Crystal structure p-loop]]
| + | |
| - | [[Category: Histone macroh2a]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Macro_h2a domain-hydrolase complex]]
| + | |
| - | [[Category: Macro_h2a domain/hydrolase]]
| + | |
| - | [[Category: Nucleotide]]
| + | |
| Structural highlights
Function
Y1521_ARCFU Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1-phosphate (Appr1p), but with low efficiency.[1] [2]
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 PubMed
The ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose.
The macro domain is an ADP-ribose binding module.,Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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
- ↑ Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG. The macro domain is an ADP-ribose binding module. EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274
- ↑ Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG. The macro domain is an ADP-ribose binding module. EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274
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