7XAY
Crystal structure of Hat1-Hat2-Asf1-H3-H4
Summary for 7XAY
| Entry DOI | 10.2210/pdb7xay/pdb |
| Descriptor | Soluble cytochrome b562,Histone acetyltransferase type B catalytic subunit, Histone acetyltransferase type B subunit 2, Histone chaperone asf1, ... (6 entities in total) |
| Functional Keywords | histone acetyltransferase, histones, enzymatic activity, histone chaperone, transferase |
| Biological source | Saccharomyces cerevisiae S288C More |
| Total number of polymer chains | 5 |
| Total formula weight | 137609.16 |
| Authors | Yue, Y.,Yang, W.S.,Xu, R.M. (deposition date: 2022-03-19, release date: 2022-05-18, Last modification date: 2023-11-29) |
| Primary citation | Yue, Y.,Yang, W.S.,Zhang, L.,Liu, C.P.,Xu, R.M. Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex. Genes Dev., 36:408-413, 2022 Cited by PubMed Abstract: Chaperones influence histone conformation and intermolecular interaction in multiprotein complexes, and the structures obtained with full-length histones often provide more accurate and comprehensive views. Here, our structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4 shows that the core domains of H3 and H4 are involved in binding Hat1 and Hat2, and the N-terminal tail of H3 makes extensive interaction with Hat2. These findings expand the knowledge about histone-protein interaction and implicate a function of Hat2/RbAp46/48, which is a versatile histone chaperone found in many chromatin-associated complexes, in the passing of histones between chaperones. PubMed: 35393344DOI: 10.1101/gad.349099.121 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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