5HJC

BRD3 second bromodomain in complex with histone H3 acetylation at K18

Summary for 5HJC

• Entry DOI: 10.2210/pdb5hjc/pdb
• Related: 5HJB 5HJD
• Descriptor: Bromodomain-containing protein 3, peptide of Histone H3.1, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: complex, brd3, bromodomain, histone peptide, acetyllysine, h3k18, signaling protein-peptide complex, signaling protein/peptide
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q15059 P68431
• Total number of polymer chains: 2
• Total formula weight: 14185.85

Authors

Li, Y.Y.,Zhao, D.,Guan, H.P.,Li, H.T. (deposition date: 2016-01-13, release date: 2016-04-20, Last modification date: 2024-11-13)

Primary citation

Li, Y.Y.,Sabari, B.R.,Panchenko, T.,Wen, H.,Zhao, D.,Guan, H.P.,Wan, L.,Huang, H.,Tang, Z.,Zhao, Y.,Roeder, R.G.,Shi, X.,Allis, C.D.,Li, H.T.
Molecular Coupling of Histone Crotonylation and Active Transcription by AF9 YEATS Domain
Mol.Cell, 62:181-193, 2016

PubMed Abstract: Recognition of histone covalent modifications by chromatin-binding protein modules ("readers") constitutes a major mechanism for epigenetic regulation, typified by bromodomains that bind acetyllysine. Non-acetyl histone lysine acylations (e.g., crotonylation, butyrylation, propionylation) have been recently identified, but readers that prefer these acylations have not been characterized. Here we report that the AF9 YEATS domain displays selectively higher binding affinity for crotonyllysine over acetyllysine. Structural studies revealed an extended aromatic sandwiching cage with crotonyl specificity arising from π-aromatic and hydrophobic interactions between crotonyl and aromatic rings. These features are conserved among the YEATS, but not the bromodomains. Using a cell-based model, we showed that AF9 co-localizes with crotonylated histone H3 and positively regulates gene expression in a YEATS domain-dependent manner. Our studies define the evolutionarily conserved YEATS domain as a family of crotonyllysine readers and specifically demonstrate that the YEATS domain of AF9 directly links histone crotonylation to active transcription.

PubMed: 27105114
DOI: 10.1016/j.molcel.2016.03.028

Experimental method

X-RAY DIFFRACTION (2.6 Å)