7aqm
From Proteopedia
(Difference between revisions)
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<StructureSection load='7aqm' size='340' side='right'caption='[[7aqm]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='7aqm' size='340' side='right'caption='[[7aqm]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[7aqm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[7aqm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Latimeria_chalumnae Latimeria chalumnae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AQM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RVK:Adenosine+5-diphosphoric+acid+beta-[(3beta,4beta-dihydroxy-5beta-methoxytetrahydrofuran-2alpha-yl)methyl]+estere'>RVK</scene> | + | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RVK:Adenosine+5-diphosphoric+acid+beta-[(3beta,4beta-dihydroxy-5beta-methoxytetrahydrofuran-2alpha-yl)methyl]+estere'>RVK</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=7aqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aqm OCA], [https://pdbe.org/7aqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aqm RCSB], [https://www.ebi.ac.uk/pdbsum/7aqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aqm 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=7aqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aqm OCA], [https://pdbe.org/7aqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aqm RCSB], [https://www.ebi.ac.uk/pdbsum/7aqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aqm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ADPRS_LATCH ADPRS_LATCH] ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine and threonine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose (PubMed:30472116). Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response (PubMed:30472116). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds (By similarity). Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (PubMed:30472116). Also hydrolyzes free poly(ADP-ribose) in mitochondria (By similarity). Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins (By similarity). Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers (By similarity).[UniProtKB:Q9NX46]<ref>PMID:30472116</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Coelacanth]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ahel, I]] | ||
| - | [[Category: Rack, J G.M]] | ||
| - | [[Category: Zorzini, V]] | ||
| - | [[Category: Adp-ribosylserine hydrolase]] | ||
| - | [[Category: Alpha-1''-o-methyl-adp ribose]] | ||
| - | [[Category: Arh3]] | ||
| - | [[Category: Hydrolase]] | ||
[[Category: Latimeria chalumnae]] | [[Category: Latimeria chalumnae]] | ||
| + | [[Category: Ahel I]] | ||
| + | [[Category: Rack JGM]] | ||
| + | [[Category: Zorzini V]] | ||
Current revision
ADP-ribosylserine hydrolase ARH3 of Latimeria chalumnae in complex with alpha-1-O-methyl-ADP-ribose (meADPr)
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