PDBsum entry 2kdp

Transcription

PDB id: 2kdp

Contents

Protein chain

71 a.a. *

Metals

_ZN

* Residue conservation analysis

PDB id:

2kdp

Name:

Transcription

Title:

Solution structure of the sap30 zinc finger motif

Structure:

Histone deacetylase complex subunit sap30. Chain: a. Synonym: sin3-associated polypeptide, 30 kda, sin3 corepressor complex subunit sap30. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sap30. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

47 models

Authors:

Y.He,R.Imhoff,A.Sahu,I.Radhakrishnan

Key ref:

Y.He et al. (2009). Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition. Nucleic Acids Res, 37, 2142-2152. PubMed id: 19223330

Date:

14-Jan-09 Release date: 17-Mar-09

Protein chain

O75446  (SAP30_HUMAN) -  Histone deacetylase complex subunit SAP30 from Homo sapiens

Seq: 220 a.a.

Struc: 71 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

Nucleic Acids Res 37:2142-2152 (2009)

PubMed id: 19223330

Solution structure of a novel zinc finger motif in the SAP30 polypeptide of the Sin3 corepressor complex and its potential role in nucleic acid recognition.

Y.He, R.Imhoff, A.Sahu, I.Radhakrishnan.

ABSTRACT

Giant chromatin-modifying complexes regulate gene transcription in eukaryotes by acting on chromatin substrates and 'setting' the histone code. The histone deacetylase (HDAC)-associated mammalian Sin3 corepressor complex regulates a wide variety of genes involved in all aspects of cellular physiology. The recruitment of the corepressor complex by transcription factors to specific regions of the genome is mediated by Sin3 as well as 10 distinct polypeptides that comprise the corepressor complex. Here we report the solution structure of a novel CCCH zinc finger (ZnF) motif in the SAP30 polypeptide, a key component of the corepressor complex. The structure represents a novel fold comprising two beta-strands and two alpha-helices with the zinc organizing center showing remote resemblance to the treble clef motif. In silico analysis of the structure revealed a highly conserved surface that is dominated by basic residues. NMR-based analysis of potential ligands for the SAP30 ZnF motif indicated a strong preference for nucleic acid substrates. We propose that the SAP30 ZnF functions as a double-stranded DNA-binding motif, thereby expanding the known functions of both SAP30 and the mammalian Sin3 corepressor complex. Our results also call into question the common assumption about the exclusion of DNA-binding core subunits within chromatin-modifying/remodeling complexes.