5U2J

MORF double PHD finger (DPF) in complex with histone H3K14bu

Summary for 5U2J

• Entry DOI: 10.2210/pdb5u2j/pdb
• Descriptor: Histone H3K14bu, Histone acetyltransferase KAT6B, ZINC ION, ... (4 entities in total)
• Functional Keywords: transcription, epigenetics, acyllysine, hydrolase
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q8WYB5
• Total number of polymer chains: 4
• Total formula weight: 28936.58

Authors

Andrews, F.H.,Klein, B.J.,Kutateladze, T.G. (deposition date: 2016-11-30, release date: 2017-04-12, Last modification date: 2025-04-02)

Primary citation

Klein, B.J.,Simithy, J.,Wang, X.,Ahn, J.,Andrews, F.H.,Zhang, Y.,Cote, J.,Shi, X.,Garcia, B.A.,Kutateladze, T.G.
Recognition of Histone H3K14 Acylation by MORF.
Structure, 25:650-654.e2, 2017

PubMed Abstract: The monocytic leukemia zinc-finger protein-related factor (MORF) is a transcriptional coactivator and a catalytic subunit of the lysine acetyltransferase complex implicated in cancer and developmental diseases. We have previously shown that the double plant homeodomain finger (DPF) of MORF is capable of binding to acetylated histone H3. Here we demonstrate that the DPF of MORF recognizes many newly identified acylation marks. The mass spectrometry study provides comprehensive analysis of H3K14 acylation states in vitro and in vivo. The crystal structure of the MORF DPF-H3K14butyryl complex offers insight into the selectivity of this reader toward lipophilic acyllysine substrates. Together, our findings support the mechanism by which the acetyltransferase MORF promotes spreading of histone acylation.

PubMed: 28286003
DOI: 10.1016/j.str.2017.02.003

Experimental method

X-RAY DIFFRACTION (1.6 Å)