8BPB
Cryo-EM structure of the human SIN3B histone deacetylase core complex at 2.8 Angstrom
Summary for 8BPB
| Entry DOI | 10.2210/pdb8bpb/pdb |
| EMDB information | 16148 |
| Descriptor | Isoform 2 of Paired amphipathic helix protein Sin3b, Histone deacetylase 2, PHD finger protein 12, ... (7 entities in total) |
| Functional Keywords | hdac, chromatin, cell cycle, transcription, gene regulation |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 226582.77 |
| Authors | Wan, M.S.M.,Muhammad, R.,Koliopolous, M.G.,Alfieri, C. (deposition date: 2022-11-16, release date: 2023-05-10, Last modification date: 2024-03-27) |
| Primary citation | Wan, M.S.M.,Muhammad, R.,Koliopoulos, M.G.,Roumeliotis, T.I.,Choudhary, J.S.,Alfieri, C. Mechanism of assembly, activation and lysine selection by the SIN3B histone deacetylase complex. Nat Commun, 14:2556-2556, 2023 Cited by PubMed Abstract: Lysine acetylation in histone tails is a key post-translational modification that controls transcription activation. Histone deacetylase complexes remove histone acetylation, thereby repressing transcription and regulating the transcriptional output of each gene. Although these complexes are drug targets and crucial regulators of organismal physiology, their structure and mechanisms of action are largely unclear. Here, we present the structure of a complete human SIN3B histone deacetylase holo-complex with and without a substrate mimic. Remarkably, SIN3B encircles the deacetylase and contacts its allosteric basic patch thereby stimulating catalysis. A SIN3B loop inserts into the catalytic tunnel, rearranges to accommodate the acetyl-lysine moiety, and stabilises the substrate for specific deacetylation, which is guided by a substrate receptor subunit. Our findings provide a model of specificity for a main transcriptional regulator conserved from yeast to human and a resource of protein-protein interactions for future drug designs. PubMed: 37137925DOI: 10.1038/s41467-023-38276-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
Download full validation report
