5GK9

Crystal structure of human HBO1 in complex with BRPF2

Summary for 5GK9

• Entry DOI: 10.2210/pdb5gk9/pdb
• Descriptor: Histone acetyltransferase KAT7, BRD1 protein, ZINC ION, ... (5 entities in total)
• Functional Keywords: hat, transferase-metal binding protein complex, transferase/metal binding protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus, nucleoplasm : O95251
• Total number of polymer chains: 2
• Total formula weight: 39130.24

Authors

Tao, Y.,Zhu, J.,Xu, S.,Ding, J. (deposition date: 2016-07-04, release date: 2017-03-29, Last modification date: 2023-11-08)

Primary citation

Tao, Y.,Zhong, C.,Zhu, J.,Xu, S.,Ding, J.
Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.
Nucleic Acids Res., 45:5707-5719, 2017

PubMed Abstract: HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit in multisubunit complexes comprising a BRPF1/2/3 or JADE1/2/3 scaffold protein, and two accessory proteins. BRPF2 has been shown to be important for the HAT activity of HBO1 toward H3K14. Here we demonstrated that BRPF2 can regulate the HAT activity of HBO1 toward free H3 and H4, and nucleosomal H3. Particularly, a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and can potentiate its activity toward H3K14. The crystal structure of the HBO1 MYST domain in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction. Our structural and functional data together indicate that the N-terminal region of BRPF2 plays an important role in the binding of HBO1 and a minor role in the binding of nucleosomes, which provide new mechanistic insights into the regulation of the HAT activity of HBO1 by BRPF2.

PubMed: 28334966
DOI: 10.1093/nar/gkx142

Experimental method

X-RAY DIFFRACTION (2.4 Å)