2NDF

Solution NMR structures of AF9 yeats domain in complex with histon H3 acetylation at K18

Summary for 2NDF

• Entry DOI: 10.2210/pdb2ndf/pdb
• Related: 2NDG
• NMR Information: BMRB: 26059
• Descriptor: Protein AF-9, Histone H3 peptide (2 entities in total)
• Functional Keywords: histone, crotonylation, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P42568
• Total number of polymer chains: 2
• Total formula weight: 17981.78

Authors

Zeng, L.,Zhou, M. (deposition date: 2016-05-19, release date: 2016-09-07, Last modification date: 2024-10-30)

Primary citation

Zhang, Q.,Zeng, L.,Zhao, C.,Ju, Y.,Konuma, T.,Zhou, M.M.
Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.
Structure, 24:1606-1612, 2016

PubMed Abstract: Histone lysine acylations play an important role in the regulation of gene transcription in chromatin. Unlike histone acetyl-lysine, molecular recognition of a recently identified crotonyl-lysine mark is much less understood. Here, we report that the YEATS domain of AF9 preferentially binds crotonyl-lysine over acetyl-lysine in histone H3. Nuclear magnetic resonance structural analysis reveals that crotonyl-lysine of histone H3 lysine 18 is engulfed deep in an aromatic cage of the YEATS domain where the carbonyl oxygen of crotonyl-lysine forms a hydrogen bond with the backbone amide of protein residue Tyr78. The crotonyl-lysine, through its unique electron-rich double-bond side chain, engages π-π aromatic stacking and extended hydrophobic/aromatic interactions with the YEATS domain compared with acetyl-lysine. Our mutational analysis confirmed key protein residues Phe59 and Tyr78 for crotonyl-lysine recognition. Importantly, our findings present a new structural mechanism of protein-protein interactions mediated by histone lysine crotonylation, and show how the cells interpret acyl-lysine marks in different biological contexts.

PubMed: 27545619
DOI: 10.1016/j.str.2016.05.023

Experimental method

SOLUTION NMR