3C9K
Model of Histone Octamer Tubular Crystals
Summary for 3C9K
| Entry DOI | 10.2210/pdb3c9k/pdb |
| Related | 2HIO |
| EMDB information | 1469 |
| Descriptor | Histone H2A-IV, Histone H2B 7, Histone H3.2, ... (4 entities in total) |
| Functional Keywords | helix, tubular crystal, chromosomal protein, nucleosome core, nucleus, phosphoprotein, methylation, dna binding protein |
| Biological source | Gallus gallus (Chicken) More |
| Total number of polymer chains | 8 |
| Total formula weight | 108510.80 |
| Authors | Frouws, T.D. (deposition date: 2008-02-16, release date: 2009-01-06, Last modification date: 2024-03-13) |
| Primary citation | Frouws, T.D.,Patterton, H.G.,Sewell, B.T. Histone octamer helical tubes suggest that an internucleosomal four-helix bundle stabilizes the chromatin fiber Biophys.J., 96:3363-3371, 2009 Cited by PubMed Abstract: A major question in chromatin involves the exact organization of nucleosomes within the 30-nm chromatin fiber and its structural determinants of assembly. Here we investigate the structure of histone octamer helical tubes via the method of iterative helical real-space reconstruction. Accurate placement of the x-ray structure of the histone octamer within the reconstructed density yields a pseudoatomic model for the entire helix, and allows precise identification of molecular interactions between neighboring octamers. One such interaction that would not be obscured by DNA in the nucleosome consists of a twofold symmetric four-helix bundle formed between pairs of H2B-alpha3 and H2B-alphaC helices of neighboring octamers. We believe that this interface can act as an internucleosomal four-helix bundle within the context of the chromatin fiber. The potential relevance of this interface in the folding of the 30-nm chromatin fiber is discussed. PubMed: 19383479DOI: 10.1016/j.bpj.2008.10.075 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
Download full validation report
