PDBsum entry 4qyl

Protein binding

PDB id: 4qyl

Contents

Protein chains

117 a.a.

Ligands

SER-GLY-ARG-GLY-ALY-GLN-GLY-GLY-LYS-ALA ×4

SO4 ×4

Waters ×722

PDB id:

4qyl

Name:

Protein binding

Title:

Crystal structure of the human brpf1 bromodomain in complex with a histone h2ak5ac peptide

Structure:

Peregrin. Chain: a, b, c, d. Fragment: bromodomain (unp residues 629-742). Synonym: bromodomain and phd finger-containing protein 1, protein br140. Engineered: yes. Histone h2a type 1. Chain: e, f, g, h. Fragment: histone h2ak5ac peptide (unp residues 2-13).

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: br140, brpf1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 9606

Resolution:

1.80Å R-factor: 0.206 R-free: 0.253

Authors:

M.Y.Lubula,K.C.Glass

Key ref:

M.Y.Lubula et al. (2014). Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain. Febs Lett, 588, 3844-3854. PubMed id: 25281266 DOI: 10.1016/j.febslet.2014.09.028

Date:

24-Jul-14 Release date: 24-Sep-14

Protein chains

P55201  (BRPF1_HUMAN) -  Peregrin from Homo sapiens

Seq: 1214 a.a.

Struc: 117 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.febslet.2014.09.028

Febs Lett 588:3844-3854 (2014)

PubMed id: 25281266

Structural insights into recognition of acetylated histone ligands by the BRPF1 bromodomain.

M.Y.Lubula, B.E.Eckenroth, S.Carlson, A.Poplawski, M.Chruszcz, K.C.Glass.

ABSTRACT

Bromodomain-PHD finger protein 1 (BRPF1) is part of the MOZ HAT complex and contains a unique combination of domains typically found in chromatin-associated factors, which include plant homeodomain (PHD) fingers, a bromodomain and a proline-tryptophan-tryptophan-proline (PWWP) domain. Bromodomains are conserved structural motifs generally known to recognize acetylated histones, and the BRPF1 bromodomain preferentially selects for H2AK5ac, H4K12ac and H3K14ac. We solved the X-ray crystal structures of the BRPF1 bromodomain in complex with the H2AK5ac and H4K12ac histone peptides. Site-directed mutagenesis on residues in the BRPF1 bromodomain-binding pocket was carried out to investigate the contribution of specific amino acids on ligand binding. Our results provide critical insights into the molecular mechanism of ligand binding by the BRPF1 bromodomain, and reveal that ordered water molecules are an essential component driving ligand recognition.