5XPC
Crystal Structure of Drep4 CIDE domain
Summary for 5XPC
| Entry DOI | 10.2210/pdb5xpc/pdb |
| Descriptor | DNAation factor-related protein 4, GLYCEROL (3 entities in total) |
| Functional Keywords | apoptosis, energy metabolism, dna fragmentation factor, drep4, cide |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 5 |
| Total formula weight | 57188.23 |
| Authors | Park, H.H.,Jeong, J.H. (deposition date: 2017-06-01, release date: 2017-07-26, Last modification date: 2023-11-22) |
| Primary citation | Choi, J.Y.,Qiao, Q.,Hong, S.H.,Kim, C.M.,Jeong, J.H.,Kim, Y.G.,Jung, Y.K.,Wu, H.,Park, H.H. CIDE domains form functionally important higher-order assemblies for DNA fragmentation. Proc. Natl. Acad. Sci. U.S.A., 114:7361-7366, 2017 Cited by PubMed Abstract: Cell death-inducing DFF45-like effector (CIDE) domains, initially identified in apoptotic nucleases, form a family with diverse functions ranging from cell death to lipid homeostasis. Here we show that the CIDE domains of and human apoptotic nucleases Drep2, Drep4, and DFF40 all form head-to-tail helical filaments. Opposing positively and negatively charged interfaces mediate the helical structures, and mutations on these surfaces abolish nuclease activation for apoptotic DNA fragmentation. Conserved filamentous structures are observed in CIDE family members involved in lipid homeostasis, and mutations on the charged interfaces compromise lipid droplet fusion, suggesting that CIDE domains represent a scaffold for higher-order assembly in DNA fragmentation and other biological processes such as lipid homeostasis. PubMed: 28652364DOI: 10.1073/pnas.1705949114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.902 Å) |
Structure validation
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