PDBsum entry 5erc

Transcription

PDB id: 5erc

Contents

Protein chain

167 a.a.

Metals

_CA

_ZN ×5

Waters ×156

PDB id:

5erc

Name:

Transcription

Title:

X-ray crystal structure of brpf1 pzp domain

Structure:

Peregrin. Chain: a. Fragment: pzp domain (unp residues 274-450). Synonym: bromodomain and phd finger-containing protein 1,protein br140. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: brpf1, br140. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.05Å R-factor: 0.165 R-free: 0.193

Authors:

B.J.Klein,F.H.Andrews,T.G.Kutateladze

Key ref:

B.J.Klein et al. (2016). Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation. Nucleic Acids Res, 44, 472-484. PubMed id: 26626149 DOI: 10.1093/nar/gkv1321

Date:

13-Nov-15 Release date: 30-Dec-15

Protein chain

P55201  (BRPF1_HUMAN) -  Peregrin from Homo sapiens

Seq: 1214 a.a.

Struc: 167 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gkv1321

Nucleic Acids Res 44:472-484 (2016)

PubMed id: 26626149

Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.

B.J.Klein, U.M.Muthurajan, M.E.Lalonde, M.D.Gibson, F.H.Andrews, M.Hepler, S.Machida, K.Yan, H.Kurumizaka, M.G.Poirier, J.Côté, K.Luger, T.G.Kutateladze.

ABSTRACT

BRPF1 (bromodomain PHD finger 1) is a core subunit of the MOZ histone acetyltransferase (HAT) complex, critical for normal developmental programs and implicated in acute leukemias. BRPF1 contains a unique assembly of zinc fingers, termed a PZP domain, the physiological role of which remains unclear. Here, we elucidate the structure-function relationship of this novel epigenetic reader and detail the biological and mechanistic consequences of its interaction with nucleosomes. PZP has a globular architecture and forms a 2:1 stoichiometry complex with the nucleosome, bivalently interacting with histone H3 and DNA. This binding impacts the nucleosome dynamics, shifting the DNA unwrapping/rewrapping equilibrium toward the unwrapped state and increasing DNA accessibility. We demonstrate that the DNA-binding function of the BRPF1 PZP domain is required for the MOZ-BRPF1-ING5-hEaf6 HAT complex to be recruited to chromatin and to acetylate nucleosomal histones. Our findings reveal a novel link between chromatin dynamics and MOZ-mediated acetylation.