PDBsum entry 5fxy

Transcription

PDB id: 5fxy

Contents

Protein chains

381 a.a.

69 a.a.

68 a.a.

PDB id:

5fxy

Name:

Transcription

Title:

Structure of the human rbbp4:mta1(464-546) complex

Structure:

Histone-binding protein rbbp4. Chain: a, c, e, g. Synonym: chromatin assembly factor 1 subunit c, caf-1 subunit c, chr omatin assembly factor i p48 subunit, caf-i 48 kda subunit, caf-i p48, nucleosome-remodeling factor subunit rbap48, retinoblastoma-b inding protein 4, rbbp-4, retinoblastoma-binding protein p48, rbbp 4. Engineered: yes. Metastasis-associated protein mta1. Chain: b, d, f, h.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293f.

Resolution:

3.20Å R-factor: 0.251 R-free: 0.291

Authors:

C.J.Millard,N.Varma,L.Fairall,J.W.R.Schwabe

Key ref:

C.J.Millard et al. (2016). The structure of the core NuRD repression complex provides insights into its interaction with chromatin. Elife, 5, e13941. PubMed id: 27098840 DOI: 10.7554/eLife.13941

Date:

03-Mar-16 Release date: 18-May-16

Protein chains

Q09028  (RBBP4_HUMAN) -  Histone-binding protein RBBP4 from Homo sapiens

Seq: 425 a.a.

Struc: 381 a.a.

Protein chains

Q13330  (MTA1_HUMAN) -  Metastasis-associated protein MTA1 from Homo sapiens

Seq: 715 a.a.

Struc: 69 a.a.

Protein chain

Q13330  (MTA1_HUMAN) -  Metastasis-associated protein MTA1 from Homo sapiens

Seq: 715 a.a.

Struc: 68 a.a.

DOI no: 10.7554/eLife.13941

Elife 5:e13941 (2016)

PubMed id: 27098840

The structure of the core NuRD repression complex provides insights into its interaction with chromatin.

C.J.Millard, N.Varma, A.Saleh, K.Morris, P.J.Watson, A.R.Bottrill, L.Fairall, C.J.Smith, J.W.Schwabe.

ABSTRACT

The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities. The complex regulates the higher-order structure of chromatin, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation. HDACs 1 and 2 are recruited by the MTA1 corepressor to form the catalytic core of the complex. The histone chaperone protein RBBP4, has previously been shown to bind to the carboxy-terminal tail of MTA1. We show that MTA1 recruits a second copy of RBBP4. The crystal structure reveals an extensive interface between MTA1 and RBBP4. An EM structure, supported by SAXS and crosslinking, reveals the architecture of the dimeric HDAC1:MTA1:RBBP4 assembly which forms the core of the NuRD complex. We find evidence that in this complex RBBP4 mediates interaction with histone H3 tails, but not histone H4, suggesting a mechanism for recruitment of the NuRD complex to chromatin.