PDBsum entry 4yyi

Protein binding

PDB id: 4yyi

Contents

Protein chains

100 a.a.

Ligands

GLY-ALY-GLY-GLY-ALY-GLY ×2

Waters ×287

PDB id:

4yyi

Name:

Protein binding

Title:

Crystal structure of brd9 bromodomain bound to an acetylated peptide

Structure:

Bromodomain-containing protein 9. Chain: a, b, d, e. Fragment: bromodomain (unp residues 17-123). Synonym: rhabdomyosarcoma antigen mu-rms-40.8, brd9. Engineered: yes. Histone h4. Chain: c, f. Fragment: n-terminal tail (unp residues 2-12). Engineered: yes.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: brd9, unq3040/pro9856. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 9606

Resolution:

1.50Å R-factor: 0.208 R-free: 0.242

Authors:

Y.Tang,S.Bellon,A.G.Cochran,F.Poy

Key ref:

E.M.Flynn et al. (2015). A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications. Structure, 23, 1801-1814. PubMed id: 26365797 DOI: 10.1016/j.str.2015.08.004

Date:

23-Mar-15 Release date: 16-Sep-15

Protein chains

Q9H8M2  (BRD9_HUMAN) -  Bromodomain-containing protein 9 from Homo sapiens

Seq: 597 a.a.

Struc: 100 a.a.

DOI no: 10.1016/j.str.2015.08.004

Structure 23:1801-1814 (2015)

PubMed id: 26365797

A Subset of Human Bromodomains Recognizes Butyryllysine and Crotonyllysine Histone Peptide Modifications.

E.M.Flynn, O.W.Huang, F.Poy, M.Oppikofer, S.F.Bellon, Y.Tang, A.G.Cochran.

ABSTRACT

Bromodomains are epigenetic readers that are recruited to acetyllysine residues in histone tails. Recent studies have identified non-acetyl acyllysine modifications, raising the possibility that these might be read by bromodomains. Profiling the nearly complete human bromodomain family revealed that while most human bromodomains bind only the shorter acetyl and propionyl marks, the bromodomains of BRD9, CECR2, and the second bromodomain of TAF1 also recognize the longer butyryl mark. In addition, the TAF1 second bromodomain is capable of binding crotonyl marks. None of the human bromodomains tested binds succinyl marks. We characterized structurally and biochemically the binding to different acyl groups, identifying bromodomain residues and structural attributes that contribute to specificity. These studies demonstrate a surprising degree of plasticity in some human bromodomains but no single factor controlling specificity across the family. The identification of candidate butyryl- and crotonyllysine readers supports the idea that these marks could have specific physiological functions.