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5IOK

Crystal structure of Taf14 YEATS domain in complex with histone H3K9cr

Summary for 5IOK
Entry DOI10.2210/pdb5iok/pdb
DescriptorTranscription initiation factor TFIID subunit 14, (ACE)QTAR(KCR)ST, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
Functional Keywordscrotonylation, crotonyllysine, epigenetics, reader, histone h3, h3k9cr, transcription
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Cellular locationNucleus: P35189
Total number of polymer chains2
Total formula weight17278.72
Authors
Andrews, F.H.,Kuateladze, T.G. (deposition date: 2016-03-08, release date: 2016-04-20, Last modification date: 2023-11-15)
Primary citationAndrews, 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: 27089029
DOI: 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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