6Z6P

HDAC-PC-Nuc

Summary for 6Z6P

• Entry DOI: 10.2210/pdb6z6p/pdb
• EMDB information: 11102
• Descriptor: Histone deacetylase HDA1, Histone H4, Histone H2A type 1, ... (15 entities in total)
• Functional Keywords: protein complex, gene regulation
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); More
• Total number of polymer chains: 14
• Total formula weight: 460635.05

Authors

Lee, J.-H.,Bollschweiler, D.,Schaefer, T.,Huber, R. (deposition date: 2020-05-28, release date: 2021-02-17, Last modification date: 2024-11-20)

Primary citation

Lee, J.H.,Bollschweiler, D.,Schafer, T.,Huber, R.
Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies.
Sci Adv, 7:-, 2021

PubMed Abstract: The chromatin-modifying histone deacetylases (HDACs) remove acetyl groups from acetyl-lysine residues in histone amino-terminal tails, thereby mediating transcriptional repression. Structural makeup and mechanisms by which multisubunit HDAC complexes recognize nucleosomes remain elusive. Our cryo-electron microscopy structures of the yeast class II HDAC ensembles show that the HDAC protomer comprises a triangle-shaped assembly of stoichiometry Hda1-Hda2-Hda3, in which the active sites of the Hda1 dimer are freely accessible. We also observe a tetramer of protomers, where the nucleosome binding modules are inaccessible. Structural analysis of the nucleosome-bound complexes indicates how positioning of Hda1 adjacent to histone H2B affords HDAC catalysis. Moreover, it reveals how an intricate network of multiple contacts between a dimer of protomers and the nucleosome creates a platform for expansion of the HDAC activities. Our study provides comprehensive insight into the structural plasticity of the HDAC complex and its functional mechanism of chromatin modification.

PubMed: 33523989
DOI: 10.1126/sciadv.abd4413

Experimental method

ELECTRON MICROSCOPY (4.43 Å)