5FXY

Structure of the human RBBP4:MTA1(464-546) complex

Summary for 5FXY

• Entry DOI: 10.2210/pdb5fxy/pdb
• Descriptor: HISTONE-BINDING PROTEIN RBBP4, METASTASIS-ASSOCIATED PROTEIN MTA1 (2 entities in total)
• Functional Keywords: transcription, transcription repression complex metastasis associated complex mta1 rbbp4 rbbp7 histone binding protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: Q09028; Isoform Short: Cytoplasm. Isoform Long: Nucleus: Q13330
• Total number of polymer chains: 8
• Total formula weight: 229932.34

Authors

Millard, C.J.,Varma, N.,Fairall, L.,Schwabe, J.W.R. (deposition date: 2016-03-03, release date: 2016-05-18, Last modification date: 2024-01-10)

Primary citation

Millard, C.J.,Varma, N.,Saleh, A.,Morris, K.,Watson, P.J.,Bottrill, A.R.,Fairall, L.,Smith, C.J.,Schwabe, J.W.
The structure of the core NuRD repression complex provides insights into its interaction with chromatin.
Elife, 5:e13941-e13941, 2016

PubMed 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.

PubMed: 27098840
DOI: 10.7554/eLife.13941

Experimental method

X-RAY DIFFRACTION (3.2 Å)