5D7E: Crystal Structure Of Taf14 Yeats Domain In Complex With H3k9ac

The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. Our findings establish a highly conserved acetyllysine reader function for the YEATS domain protein family and highlight the significance of this interaction for Taf14.
PDB ID: 5D7EDownload
MMDB ID: 132969
PDB Deposition Date: 2015/8/13
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Saccharomyces cerevisiae S288C
Similar Structures:
Biological Unit for 5D7E: dimeric; determined by author and by software (PISA)
Molecular Components in 5D7E
Label Count Molecule
Proteins (2 molecules)
Transcription Initiation Factor Tfiid Subunit 14(Gene symbol: TAF14)
Molecule annotation
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB