5D7E
Crystal structure of Taf14 YEATS domain in complex with H3K9ac
Summary for 5D7E
| Entry DOI | 10.2210/pdb5d7e/pdb |
| Descriptor | Transcription initiation factor TFIID subunit 14, H3K9ac, DI(HYDROXYETHYL)ETHER, ... (5 entities in total) |
| Functional Keywords | acetylation histone yeats reader, nuclear protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 17444.92 |
| Authors | Andrews, F.H.,Shanle, E.K.,Strahl, B.D.,Kutateladze, T.G. (deposition date: 2015-08-13, release date: 2015-09-23, Last modification date: 2024-10-09) |
| Primary citation | Shanle, E.K.,Andrews, F.H.,Meriesh, H.,McDaniel, S.L.,Dronamraju, R.,DiFiore, J.V.,Jha, D.,Wozniak, G.G.,Bridgers, J.B.,Kerschner, J.L.,Krajewski, K.,Martin, G.M.,Morrison, A.J.,Kutateladze, T.G.,Strahl, B.D. Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response. Genes Dev., 29:1795-1800, 2015 Cited by PubMed Abstract: 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. PubMed: 26341557DOI: 10.1101/gad.269977.115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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