PDBsum entry 1uz3

Chromatin regulator

PDB id: 1uz3

Contents

Protein chains

102 a.a. *

97 a.a. *

Waters ×358

* Residue conservation analysis

PDB id:

1uz3

Name:

Chromatin regulator

Title:

Crystal structure of novel protein emsy

Structure:

Emsy protein. Chain: a, b. Fragment: residues 1-100. Engineered: yes

Source:

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

Biol. unit:

Dimer (from PDB file)

Resolution:

1.10Å R-factor: 0.145 R-free: 0.199

Authors:

G.B.Chavali,B.P.Basu,A.J.Doherty

Key ref:

G.B.Chavali et al. (2005). Crystal structure of the ENT domain of human EMSY. J Mol Biol, 350, 964-973. PubMed id: 15978617 DOI: 10.1016/j.jmb.2005.05.047

Date:

03-Mar-04 Release date: 13-Oct-05

Protein chain

Q7Z589  (EMSY_HUMAN) -  BRCA2-interacting transcriptional repressor EMSY from Homo sapiens

Seq: 1322 a.a.

Struc: 102 a.a.

Protein chain

Q7Z589  (EMSY_HUMAN) -  BRCA2-interacting transcriptional repressor EMSY from Homo sapiens

Seq: 1322 a.a.

Struc: 97 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1016/j.jmb.2005.05.047

J Mol Biol 350:964-973 (2005)

PubMed id: 15978617

Crystal structure of the ENT domain of human EMSY.

G.B.Chavali, C.M.Ekblad, B.P.Basu, N.C.Brissett, D.Veprintsev, L.Hughes-Davies, T.Kouzarides, L.S.Itzhaki, A.J.Doherty.

ABSTRACT

EMSY is a recently discovered gene encoding a BRCA2-associated protein and is amplified in some sporadic breast and ovarian cancers. The EMSY sequence contains no known domain except for a conserved approximately 100 residue segment at the N terminus. This so-called ENT domain is unique in the human genome, although multiple copies are found in Arabidopsis proteins containing members of the Royal family of chromatin remodelling domains. Here, we report the crystal structure of the ENT domain of EMSY, consisting of a unique arrangement of five alpha-helices that fold into a helical bundle arrangement. The fold shares regions of structural homology with the DNA-binding domain of homeodomain proteins. The ENT domain forms a homodimer via the anti-parallel packing of the extended N-terminal alpha-helix of each molecule. It is stabilized mainly by hydrophobic residues at the dimer interface and has a dissociation constant in the low micromolar range. The dimerisation of EMSY mediated by the ENT domain could provide flexibility for it to bind two or more different substrates simultaneously.

Selected figure(s)

Figure 3.
Figure 3. Structure of the ENT domain of EMSY. Crystal structure of the ENT monomer showing the helical bundle fold formed by the five helices in the molecule.

Figure 4.
Figure 4. Structure of the homodimeric complex of ENT domains. (a) The secondary structure of EMSY1--100 showing the two monomers A and B in pink and blue, respectively. The a-helices from chain A are denoted as a1-a5 and from chain B as a10-a50. (b) The salt-bridges and hydrogen bonds, indicated by dotted lines, stabilizing the dimer visualized using POVSCRIPTC. 25 (c) Molecular surface representation of the ENT homodimer. A Coulomb method using only charged residues was used to calculate the electrostatic potential, which was mapped to the molecular surface with red representing negative charge and blue representing positive charge. The Figure was prepared using SwissPdb Viewer. 26

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 350, 964-973) copyright 2005.

Figures were selected by the author.