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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 DohertyEMSY 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 BiologyISSN
0022-2836External DOI
Issue
5Volume
350Page range
964-973Pages
10.0Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Full text available
- No
Peer reviewed?
- Yes