4qn0: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qn0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QN0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qn0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QN0 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></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]] 2.74Å</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></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=4qn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qn0 OCA], [https://pdbe.org/4qn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qn0 RCSB], [https://www.ebi.ac.uk/pdbsum/4qn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qn0 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=4qn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qn0 OCA], [https://pdbe.org/4qn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qn0 RCSB], [https://www.ebi.ac.uk/pdbsum/4qn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qn0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 18:08, 8 November 2023
Crystal structure of the CPS-6 mutant Q130KCrystal structure of the CPS-6 mutant Q130K
Structural highlights
FunctionNUCG_CAEEL Endonuclease important for programmed cell death; it mediates apoptotic DNA fragmentation. Publication Abstract from PubMedEndonuclease G (EndoG) is a mitochondrial protein that is released from mitochondria and relocated into the nucleus to promote chromosomal DNA fragmentation during apoptosis. Here, we show that oxidative stress causes cell-death defects in C. elegans through an EndoG-mediated cell-death pathway. In response to high reactive oxygen species (ROS) levels, homodimeric CPS-6-the C. elegans homolog of EndoG-is dissociated into monomers with diminished nuclease activity. Conversely, the nuclease activity of CPS-6 is enhanced, and its dimeric structure is stabilized by its interaction with the worm AIF homolog, WAH-1, which shifts to disulfide cross-linked dimers under high ROS levels. CPS-6 thus acts as a ROS sensor to regulate the life and death of cells. Modulation of the EndoG dimer conformation could present an avenue for prevention and treatment of diseases resulting from oxidative stress. Oxidative Stress Impairs Cell Death by Repressing the Nuclease Activity of Mitochondrial Endonuclease G.,Lin JL, Nakagawa A, Skeen-Gaar R, Yang WZ, Zhao P, Zhang Z, Ge X, Mitani S, Xue D, Yuan HS Cell Rep. 2016 Jul 12;16(2):279-87. doi: 10.1016/j.celrep.2016.05.090. Epub 2016 , Jun 23. PMID:27346342[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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