PDBsum entry: 1ap0

Chromatin-binding

PDB id: 1ap0

Contents

Protein chain

73 a.a. *

* Residue conservation analysis

PDB id:

1ap0

Name:

Chromatin-binding

Title:

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1, nmr, 26 structures

Structure:

Modifier protein 1. Chain: a. Fragment: chromatin-binding (chromo), residues 10 - 80. Synonym: momod1, heterochromatin protein 1. Engineered: yes. Mutation: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Cell_line: bl21. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

26 models

Authors:

L.J.Ball,N.V.Murzina,R.W.Broadhurst,A.R.C.Raine,S.J.Archer, F.J.Stott,A.G.Murzin,P.B.Singh,P.J.Domaille,E.D.Laue

Key ref:

L.J.Ball et al. (1997). Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. EMBO J, 16, 2473-2481. PubMed id: 9171360 DOI: 10.1093/emboj/16.9.2473

Date:

22-Jul-97 Release date: 22-Jul-98

Protein chain

P83917  (CBX1_MOUSE) -  Chromobox protein homolog 1

Seq: 185 a.a.

Struc: 73 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (2 terms)
• Biological process: chromatin assembly or disassembly (1 term)
• Biochemical function: chromatin binding (1 term)

DOI no: 10.1093/emboj/16.9.2473

EMBO J 16:2473-2481 (1997)

PubMed id: 9171360

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

L.J.Ball, N.V.Murzina, R.W.Broadhurst, A.R.Raine, S.J.Archer, F.J.Stott, A.G.Murzin, P.B.Singh, P.J.Domaille, E.D.Laue.

ABSTRACT

The structure of a chromatin binding domain from mouse chromatin modifier protein 1 (MoMOD1) was determined using nuclear magnetic resonance (NMR) spectroscopy. The protein consists of an N-terminal three-stranded anti-parallel beta-sheet which folds against a C-terminal alpha-helix. The structure reveals an unexpected homology to two archaebacterial DNA binding proteins which are also involved in chromatin structure. Structural comparisons suggest that chromo domains, of which more than 40 are now known, act as protein interaction motifs and that the MoMOD1 protein acts as an adaptor mediating interactions between different proteins.

Selected figure(s)

Figure 1.
Figure 1 Amino acid sequence of the MoMOD1 chromo domain showing its homology with other representative chromo domains. Selected conserved residues are coloured yellow (core hydrophobic), green (Gly and Pro) and blue (basic). See text for details.

Figure 3.
Figure 3 Location of the secondary structure in MoMOD1-N. Below the classification of the elements of secondary structure, the CSI line indicates the consensus chemical shift index for 1H[ ], 13C[ ]and 13C[ ]nuclei. The stars below the amino acid sequence represent the location of slowly exchanging amide protons. In the next rows, filled and empty circles represent residues with 3J[ N] > 9 Hz and < 4Hz respectively and squares represent residues for which [1] has been determined. Following this, three rows of solid bars represent the observed sequential d[ N], d[ N] and d[NN] NOE connectivities; the thickness of the bars indicates the intensities of the crosspeaks in the NOESY spectra. Further bars represent d[ N](i, i + 2), d[NN](i, i +2), d[ N](i, i + 3), d[ ](i, i + 3), d[NN](i, i +3) and d[ N](i, i + 4) NOE connectivities between the residues shown.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1997, 16, 2473-2481) copyright 1997.

Figures were selected by an automated process.