4QN0
Crystal structure of the CPS-6 mutant Q130K
Summary for 4QN0
| Entry DOI | 10.2210/pdb4qn0/pdb |
| Related | 3S5B |
| Descriptor | Endonuclease G, mitochondrial, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | beta-beta-alpha metal motif, endoribonuclease, mitochondrial membrane, hydrolase |
| Biological source | Caenorhabditis elegans (roundworm) |
| Cellular location | Mitochondrion : Q95NM6 |
| Total number of polymer chains | 4 |
| Total formula weight | 109686.56 |
| Authors | Lin, J.L.J.,Yuan, H.S. (deposition date: 2014-06-17, release date: 2015-06-17, Last modification date: 2023-11-08) |
| Primary citation | Lin, J.L.J.,Nakagawa, A.,Skeen-Gaar, R.,Yang, W.Z.,Zhao, P.,Zhang, Z.,Ge, X.,Mitani, S.,Xue, D.,Yuan, H.S. Oxidative Stress Impairs Cell Death by Repressing the Nuclease Activity of Mitochondrial Endonuclease G Cell Rep, 16:279-287, 2016 Cited by PubMed Abstract: Endonuclease 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. PubMed: 27346342DOI: 10.1016/j.celrep.2016.05.090 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.74 Å) |
Structure validation
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