1AOI
COMPLEX BETWEEN NUCLEOSOME CORE PARTICLE (H3,H4,H2A,H2B) AND 146 BP LONG DNA FRAGMENT
Summary for 1AOI
| Entry DOI | 10.2210/pdb1aoi/pdb |
| Descriptor | PALINDROMIC 146 BP DNA REPEAT 8/9 FROM HUMAN X-CHROMOSOME ALPHA SATELLITE DNA, HISTONE H3, HISTONE H4, ... (7 entities in total) |
| Functional Keywords | nucleosome, chromatin, histone, protein dna interaction, nucleoprotein, supercoiled dna, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Xenopus laevis (African clawed frog) More |
| Cellular location | Nucleus: P02302 P62799 P06897 P02281 |
| Total number of polymer chains | 10 |
| Total formula weight | 184547.40 |
| Authors | Luger, K.,Maeder, A.W.,Richmond, R.K.,Sargent, D.F.,Richmond, T.J. (deposition date: 1997-07-03, release date: 1998-09-30, Last modification date: 2024-02-07) |
| Primary citation | Luger, K.,Mader, A.W.,Richmond, R.K.,Sargent, D.F.,Richmond, T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature, 389:251-260, 1997 Cited by PubMed Abstract: The X-ray crystal structure of the nucleosome core particle of chromatin shows in atomic detail how the histone protein octamer is assembled and how 146 base pairs of DNA are organized into a superhelix around it. Both histone/histone and histone/DNA interactions depend on the histone fold domains and additional, well ordered structure elements extending from this motif. Histone amino-terminal tails pass over and between the gyres of the DNA superhelix to contact neighbouring particles. The lack of uniformity between multiple histone/DNA-binding sites causes the DNA to deviate from ideal superhelix geometry. PubMed: 9305837DOI: 10.1038/38444 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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