Summary for 6HTS
| Entry DOI | 10.2210/pdb6hts/pdb |
| EMDB information | 3954 |
| Descriptor | RuvB-like 1, DNA (150-MER), ADENOSINE-5'-DIPHOSPHATE, ... (13 entities in total) |
| Functional Keywords | chromatin, remodeller, nucleosome, dna binding, histones, dna repair, atpase, helicase, sliding, complex, dna binding protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 19 |
| Total formula weight | 811323.31 |
| Authors | Ayala, R.,Willhoft, O.,Aramayo, R.J.,Wilkinson, M.,McCormack, E.A.,Ocloo, L.,Wigley, D.B.,Zhang, X. (deposition date: 2018-10-04, release date: 2018-11-07, Last modification date: 2024-05-15) |
| Primary citation | Ayala, R.,Willhoft, O.,Aramayo, R.J.,Wilkinson, M.,McCormack, E.A.,Ocloo, L.,Wigley, D.B.,Zhang, X. Structure and regulation of the human INO80-nucleosome complex. Nature, 556:391-395, 2018 Cited by PubMed Abstract: Access to DNA within nucleosomes is required for a variety of processes in cells including transcription, replication and repair. Consequently, cells encode multiple systems that remodel nucleosomes. These complexes can be simple, involving one or a few protein subunits, or more complicated multi-subunit machines . Biochemical studies have placed the motor domains of several chromatin remodellers in the superhelical location 2 region of the nucleosome. Structural studies of yeast Chd1 and Snf2-a subunit in the complex with the capacity to remodel the structure of chromatin (RSC)-in complex with nucleosomes have provided insights into the basic mechanism of nucleosome sliding performed by these complexes. However, how larger, multi-subunit remodelling complexes such as INO80 interact with nucleosomes and how remodellers carry out functions such as nucleosome sliding , histone exchange and nucleosome spacing remain poorly understood. Although some remodellers work as monomers , others work as highly cooperative dimers. Here we present the structure of the human INO80 chromatin remodeller with a bound nucleosome, which reveals that INO80 interacts with nucleosomes in a previously undescribed manner: the motor domains are located on the DNA at the entry point to the nucleosome, rather than at superhelical location 2. The ARP5-IES6 module of INO80 makes additional contacts on the opposite side of the nucleosome. This arrangement enables the histone H3 tails of the nucleosome to have a role in the regulation of the activities of the INO80 motor domain-unlike in other characterized remodellers, for which H4 tails have been shown to regulate the motor domains. PubMed: 29643506DOI: 10.1038/s41586-018-0021-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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