1JEY
Crystal Structure of the Ku heterodimer bound to DNA
Summary for 1JEY
Entry DOI | 10.2210/pdb1jey/pdb |
Related | 1JEQ |
Descriptor | DNA (5'-D(*GP*TP*TP*TP*TP*TP*AP*GP*TP*TP*TP*AP*TP*TP*GP*GP*GP*CP*GP*CP*G)-3'), DNA (34-MER), Ku70, ... (5 entities in total) |
Functional Keywords | double-strand dna break repair, non-homologous end-joining, protein-nucleic acid complex, alpha/beta domain, beta barrel, helical c-terminal arm, sap domain, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus : P12956 P13010 |
Total number of polymer chains | 4 |
Total formula weight | 150967.46 |
Authors | Walker, J.R.,Corpina, R.A.,Goldberg, J. (deposition date: 2001-06-19, release date: 2001-08-10, Last modification date: 2023-08-16) |
Primary citation | Walker, J.R.,Corpina, R.A.,Goldberg, J. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature, 412:607-614, 2001 Cited by PubMed Abstract: The Ku heterodimer (Ku70 and Ku80 subunits) contributes to genomic integrity through its ability to bind DNA double-strand breaks and facilitate repair by the non-homologous end-joining pathway. The crystal structure of the human Ku heterodimer was determined both alone and bound to a 55-nucleotide DNA element at 2.7 and 2.5 A resolution, respectively. Ku70 and Ku80 share a common topology and form a dyad-symmetrical molecule with a preformed ring that encircles duplex DNA. The binding site can cradle two full turns of DNA while encircling only the central 3-4 base pairs (bp). Ku makes no contacts with DNA bases and few with the sugar-phosphate backbone, but it fits sterically to major and minor groove contours so as to position the DNA helix in a defined path through the protein ring. These features seem well designed to structurally support broken DNA ends and to bring the DNA helix into phase across the junction during end processing and ligation. PubMed: 11493912DOI: 10.1038/35088000 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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