5I3L

DPF3b in complex with H3K14ac peptide

Summary for 5I3L

• Entry DOI: 10.2210/pdb5i3l/pdb
• Descriptor: Zinc finger protein DPF3, H3K14ac peptide, ZINC ION, ... (7 entities in total)
• Functional Keywords: structural genomics, structural genomics consortium, sgc, peptide binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 28601.26

Authors

Tempel, W.,Liu, Y.,Walker, J.R.,Zhao, A.,Qin, S.,Loppnau, P.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Structural Genomics Consortium (SGC) (deposition date: 2016-02-10, release date: 2016-02-24, Last modification date: 2023-11-15)

Primary citation

Li, W.,Zhao, A.,Tempel, W.,Loppnau, P.,Liu, Y.
Crystal structure of DPF3b in complex with an acetylated histone peptide.
J.Struct.Biol., 195:365-372, 2016

PubMed Abstract: Histone acetylation plays an important role in chromatin dynamics and is associated with active gene transcription. This modification is written by acetyltransferases, erased by histone deacetylases and read out by bromodomain containing proteins, and others such as tandem PHD fingers of DPF3b. Here we report the high resolution crystal structure of the tandem PHD fingers of DPF3b in complex with an H3K14ac peptide. In the complex structure, the histone peptide adopts an α-helical conformation, unlike previously observed by NMR, but similar to a previously reported MOZ-H3K14ac complex structure. Our crystal structure adds to existing evidence that points to the α-helix as a natural conformation of histone tails as they interact with histone-associated proteins.

PubMed: 27402533
DOI: 10.1016/j.jsb.2016.07.001

Experimental method

X-RAY DIFFRACTION (1.85 Å)