3TU4
Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.
Summary for 3TU4
| Entry DOI | 10.2210/pdb3tu4/pdb |
| Descriptor | Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total) |
| Functional Keywords | histones, nucleosome, gene silencing, signaling protein-structural protein-dna complex, signaling protein/structural protein/dna |
| Biological source | Xenopus laevis (clawed frog,common platanna,platanna) More |
| Cellular location | Nucleus: P84233 P62799 P02281 3TU4 Nucleus (By similarity): Q6AZJ8 |
| Total number of polymer chains | 12 |
| Total formula weight | 253414.99 |
| Authors | Armache, K.-J.,Garlick, J.D.,Canzio, D.,Narlikar, G.J.,Kingston, R.E. (deposition date: 2011-09-15, release date: 2011-11-23, Last modification date: 2024-02-28) |
| Primary citation | Armache, K.J.,Garlick, J.D.,Canzio, D.,Narlikar, G.J.,Kingston, R.E. Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution. Science, 334:977-982, 2011 Cited by PubMed Abstract: Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component. PubMed: 22096199DOI: 10.1126/science.1210915 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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