PDBsum entry: 2fmm

Transcription

PDB id: 2fmm

Contents

Protein chains

118 a.a. *

68 a.a. *

Ligands

SO4 ×4

Waters ×386

* Residue conservation analysis

PDB id:

2fmm

Name:

Transcription

Title:

Crystal structure of emsy-hp1 complex

Structure:

Protein emsy. Chain: e. Fragment: n-terminal domain. Engineered: yes. Chromobox protein homolog 1. Chain: a, b, c, d. Fragment: chromo shadow domain. Synonym: heterochromatin protein 1 homolog beta, hp1 beta, protein, m31, heterochromatin protein p25, hp1hsbeta, p25be

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: emsy, c11orf30. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: cbx1, cbx. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Pentamer (from PDB file)

Resolution:

1.80Å R-factor: 0.219 R-free: 0.243

Authors:

Y.Huang

Key ref:

Y.Huang et al. (2006). Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1 binding. Structure, 14, 703-712. PubMed id: 16615912 DOI: 10.1016/j.str.2006.01.007

Date:

09-Jan-06 Release date: 23-May-06

Protein chain

Q7Z589  (EMSY_HUMAN) -  Protein EMSY

Seq: 1322 a.a.

Struc: 118 a.a.*

Protein chains

P83916  (CBX1_HUMAN) -  Chromobox protein homolog 1

Seq: 185 a.a.

Struc: 68 a.a.

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

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (1 term)

DOI no: 10.1016/j.str.2006.01.007

Structure 14:703-712 (2006)

PubMed id: 16615912

Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1 binding.

Y.Huang, M.P.Myers, R.M.Xu.

ABSTRACT

Heterochromatin protein-1 (HP1) plays an essential role in both the assembly of higher-order chromatin structure and epigenetic inheritance. The C-terminal chromo shadow domain (CSD) of HP1 is responsible for homodimerization and interaction with a number of chromatin-associated nonhistone proteins, including EMSY, which is a BRCA2-interacting protein that has been implicated in the development of breast and ovarian cancer. We have determined the crystal structure of the HP1beta CSD in complex with the N-terminal domain of EMSY at 1.8 A resolution. Surprisingly, the structure reveals that EMSY is bound by two HP1 CSD homodimers, and the binding sequences differ from the consensus HP1 binding motif PXVXL. This structural information expands our understanding of HP1 binding specificity and provides insights into interactions between HP1 homodimers that are likely to be important for heterochromatin formation.

Selected figure(s)

Figure 1.
Figure 1. Structure Determination
(A) A section of the MAD-phased electron density map surrounding the ENT-proximal HP1 binding site. The 2.3 Å map is shown in a filled chicken-wire representation and is contoured at the 1.0s level. The refined model of the EMSY-HP1 CSD complex (stick model) is superimposed onto the map. EMSY, HP1 CSD-A1, and HP1 CSD-A2 molecules are shown with carbon bonds colored yellow, magenta, and red, respectively.
(B) The overall structure of the EMSY-HP1 CSD complex shown in a ribbon representation. One asymmetric unit contains half of the EMSY homodimer, and the other half (shaded) is related by a 2-fold symmetry. EMSY is colored yellow, the ENT-proximal CSD dimer (CSD-A) is shown in magenta (CSD-A1) and red (CSD-A2), and the ENT-distal dimer (CSD-B) is shown in green (CSD-B1) and cyan (CSD-B2).
(C) Superposition of the backbones of CSD-A (red), CSD-B (green), and the HP1 CSD dimer of the HP1-CAF-1 complex (white).

The above figure is reprinted by permission from Cell Press: Structure (2006, 14, 703-712) copyright 2006.

Figure was selected by the author.