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Crystal structure of the ENT domain of human EMSY

journal contribution
posted on 2023-06-07, 19:16 authored by Gayatri B Chavali, Caroline M S Ekblad, Balaka P Basu, Nigel Brissett, Dmitry Veprintsev, Luke Hughes-Davies, Tony Kouzarides, Laura S Itzhaki, Aidan DohertyAidan Doherty
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 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 a-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 a-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.

History

Publication status

  • Published

Journal

Journal of Molecular Biology

ISSN

0022-2836

Issue

5

Volume

350

Page range

964-973

Pages

10.0

Department affiliated with

  • Sussex Centre for Genome Damage Stability Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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