4OZT

crystal structure of the ligand binding domains of the Bovicola ovis ecdysone receptor EcR/USP heterodimer (PonA crystal)

Summary for 4OZT

• Entry DOI: 10.2210/pdb4ozt/pdb
• Related: 4OZR
• Descriptor: Ecdysone receptor, Retinoid X receptor, 2,3,14,20,22-PENTAHYDROXYCHOLEST-7-EN-6-ONE, ... (5 entities in total)
• Functional Keywords: ecdysone receptor, usp, pona, transcription
• Biological source: Pediculus humanus subsp. corporis (Body louse); More
• Total number of polymer chains: 2
• Total formula weight: 50049.93

Authors

Ren, B.,Peat, T.S.,Streltsov, V.A.,Pollard, M.,Fernley, R.,Grusovin, J.,Seabrook, S.,Pilling, P.,Phan, T.,Lu, L.,Lovrecz, G.O.,Graham, L.D.,Hill, R.J. (deposition date: 2014-02-19, release date: 2014-07-30, Last modification date: 2023-12-27)

Primary citation

Ren, B.,Peat, T.S.,Streltsov, V.A.,Pollard, M.,Fernley, R.,Grusovin, J.,Seabrook, S.,Pilling, P.,Phan, T.,Lu, L.,Lovrecz, G.O.,Graham, L.D.,Hill, R.J.
Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits.
Acta Crystallogr.,Sect.D, 70:1954-1964, 2014

PubMed Abstract: The heterodimeric ligand-binding region of the Bovicola ovis ecdysone receptor has been crystallized either in the presence of an ecdysteroid or a synthetic methylene lactam insecticide. Two X-ray crystallographic structures, determined at 2.7 Å resolution, show that the ligand-binding domains of both subunits of this receptor, like those of other nuclear receptors, can display significant conformational flexibility. Thermal melt experiments show that while ponasterone A stabilizes the higher order structure of the heterodimer in solution, the methylene lactam destabilizes it. The conformations of the EcR and USP subunits observed in the structure crystallized in the presence of the methylene lactam have not been seen previously in any ecdysone receptor structure and represent a new level of conformational flexibility for these important receptors. Interestingly, the new USP conformation presents an open, unoccupied ligand-binding pocket.

PubMed: 25004972
DOI: 10.1107/S1399004714009626

Experimental method

X-RAY DIFFRACTION (2.7 Å)