5J9T

Crystal structure of the NuA4 core complex

Summary for 5J9T

• Entry DOI: 10.2210/pdb5j9t/pdb
• Related: 5J9Q 5J9U 5J9W
• Descriptor: Histone acetyltransferase ESA1, Chromatin modification-related protein EAF6, Enhancer of polycomb-like protein 1, ... (5 entities in total)
• Functional Keywords: nua4, nucleosome, histone, acetylation, transferase
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Nucleus : P47128 P43572 P38806
• Total number of polymer chains: 12
• Total formula weight: 289866.08

Authors

Chen, Z.C.,Xu, P. (deposition date: 2016-04-11, release date: 2016-10-26, Last modification date: 2024-10-16)

Primary citation

Xu, P.,Li, C.,Chen, Z.,Jiang, S.,Fan, S.,Wang, J.,Dai, J.,Zhu, P.,Chen, Z.
The NuA4 Core Complex Acetylates Nucleosomal Histone H4 through a Double Recognition Mechanism
Mol.Cell, 63:965-975, 2016

PubMed Abstract: NuA4 catalyzes the acetylation of nucleosomes at histone H4, which is a well-established epigenetic event, controlling many genomic processes in Saccharomyces cerevisiae. Here we report the crystal structures of the NuA4 core complex and a cryoelectron microscopy structure with the nucleosome. The structures show that the histone-binding pocket of the enzyme is rearranged, suggesting its activation. The enzyme binds the histone tail mainly through the target lysine residue, with a preference for a small residue at the -1 position. The complex engages the nucleosome at the dish face and orients its catalytic pocket close to the H4 tail to achieve selective acetylation. The combined data reveal a space-sequence double recognition mechanism of the histone tails by a modifying enzyme in the context of the nucleosome.

PubMed: 27594449
DOI: 10.1016/j.molcel.2016.07.024

Experimental method

X-RAY DIFFRACTION (2.7 Å)