8DEI
Structure of the Cac1 KER domain
Summary for 8DEI
| Entry DOI | 10.2210/pdb8dei/pdb |
| Descriptor | Maltodextrin-binding protein,Chromatin assembly factor 1 subunit p90 fusion, DI(HYDROXYETHYL)ETHER, PHOSPHATE ION, ... (5 entities in total) |
| Functional Keywords | chromatin, dna binding, dna binding protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 223150.35 |
| Authors | Rosas, R.,Churchill, M.E.A. (deposition date: 2022-06-20, release date: 2023-07-05, Last modification date: 2024-02-14) |
| Primary citation | Rosas, R.,Aguilar, R.R.,Arslanovic, N.,Seck, A.,Smith, D.J.,Tyler, J.K.,Churchill, M.E.A. A novel single alpha-helix DNA-binding domain in CAF-1 promotes gene silencing and DNA damage survival through tetrasome-length DNA selectivity and spacer function. Elife, 12:-, 2023 Cited by PubMed Abstract: The histone chaperone chromatin assembly factor 1 (CAF-1) deposits two nascent histone H3/H4 dimers onto newly replicated DNA forming the central core of the nucleosome known as the tetrasome. How CAF-1 ensures there is sufficient space for the assembly of tetrasomes remains unknown. Structural and biophysical characterization of the lysine/glutamic acid/arginine-rich (KER) region of CAF-1 revealed a 128-Å single alpha-helix (SAH) motif with unprecedented DNA-binding properties. Distinct KER sequence features and length of the SAH drive the selectivity of CAF-1 for tetrasome-length DNA and facilitate function in budding yeast. In vivo, the KER cooperates with the DNA-binding winged helix domain in CAF-1 to overcome DNA damage sensitivity and maintain silencing of gene expression. We propose that the KER SAH links functional domains within CAF-1 with structural precision, acting as a DNA-binding spacer element during chromatin assembly. PubMed: 37432722DOI: 10.7554/eLife.83538 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.81 Å) |
Structure validation
Download full validation report
