5IOK
Crystal structure of Taf14 YEATS domain in complex with histone H3K9cr
Summary for 5IOK
Entry DOI | 10.2210/pdb5iok/pdb |
Descriptor | Transcription initiation factor TFIID subunit 14, (ACE)QTAR(KCR)ST, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | crotonylation, crotonyllysine, epigenetics, reader, histone h3, h3k9cr, transcription |
Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
Cellular location | Nucleus: P35189 |
Total number of polymer chains | 2 |
Total formula weight | 17278.72 |
Authors | Andrews, F.H.,Kuateladze, T.G. (deposition date: 2016-03-08, release date: 2016-04-20, Last modification date: 2023-11-15) |
Primary citation | Andrews, F.H.,Shinsky, S.A.,Shanle, E.K.,Bridgers, J.B.,Gest, A.,Tsun, I.K.,Krajewski, K.,Shi, X.,Strahl, B.D.,Kutateladze, T.G. The Taf14 YEATS domain is a reader of histone crotonylation. Nat.Chem.Biol., 12:396-398, 2016 Cited by PubMed Abstract: The discovery of new histone modifications is unfolding at startling rates; however, the identification of effectors capable of interpreting these modifications has lagged behind. Here we report the YEATS domain as an effective reader of histone lysine crotonylation, an epigenetic signature associated with active transcription. We show that the Taf14 YEATS domain engages crotonyllysine via a unique π-π-π-stacking mechanism and that other YEATS domains have crotonyllysine-binding activity. PubMed: 27089029DOI: 10.1038/nchembio.2065 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.22 Å) |
Structure validation
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