PDBsum entry 4ljn

Transferase

PDB id: 4ljn

Contents

Protein chain

120 a.a.

Metals

_ZN ×4

Waters ×6

PDB id:

4ljn

Name:

Transferase

Title:

Crystal structure of moz double phd finger

Structure:

Histone acetyltransferase kat6a. Chain: a. Fragment: unp residues 194-323. Synonym: moz, ybf2/sas3, sas2 and tip60 protein 3, myst-3, monocytic leukemia zinc finger protein, runt-related transcription factor- binding protein 2, zinc finger protein 220. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kat6a, moz, myst3, runxbp2, znf220. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.00Å R-factor: 0.229 R-free: 0.243

Authors:

I.Dreveny,S.E.Deeves,B.Yue,D.M.Heery

Key ref:

I.Dreveny et al. (2014). The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification. Nucleic Acids Res, 42, 822-835. PubMed id: 24150941 DOI: 10.1093/nar/gkt931

Date:

05-Jul-13 Release date: 16-Oct-13

Protein chain

Q92794  (KAT6A_HUMAN) -  Histone acetyltransferase KAT6A from Homo sapiens

Seq: 2004 a.a.

Struc: 120 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.2.3.1.48 - histone acetyltransferase.
• Reaction: L-lysyl-[protein] + acetyl-CoA = N₆-acetyl-L-lysyl-[protein] + CoA + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1093/nar/gkt931

Nucleic Acids Res 42:822-835 (2014)

PubMed id: 24150941

The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.

I.Dreveny, S.E.Deeves, J.Fulton, B.Yue, M.Messmer, A.Bhattacharya, H.M.Collins, D.M.Heery.

ABSTRACT

Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sampling H3 and H4 modification status, we show that the DPF cooperates with the MYST domain to promote H3K9 and H3K14 acetylation, although not if H3K4 is trimethylated. Four crystal structures of an extended DPF alone and in complex with unmodified or acetylated forms of the H3 tail reveal the molecular basis of crosstalk between H3K4me3 and H3K14ac. We show for the first time that MOZ DPF induces α-helical conformation of H3K4-T11, revealing a unique mode of H3 recognition. The helical structure facilitates sampling of H3K4 methylation status, and proffers H3K9 and other residues for modification. Additionally, we show that a conserved double glycine hinge flanking the H3 tail helix is required for a conformational change enabling docking of H3K14ac with the DPF. In summary, our data provide the first observations of extensive helical structure in a histone tail, revealing the inherent ability of the H3 tail to adopt alternate conformations in complex with chromatin regulators.