PDBsum entry 4ozt

Transcription

PDB id: 4ozt

Contents

Protein chains

238 a.a.

195 a.a.

Ligands

P1A

NEQ

Waters ×61

PDB id:

4ozt

Name:

Transcription

Title:

Crystal structure of the ligand binding domains of the bovicola ovis ecdysone receptor ecr/usp heterodimer (pona crystal)

Structure:

Ecdysone receptor. Chain: e. Fragment: unp residues 281-518. Engineered: yes. Retinoid x receptor. Chain: u. Fragment: unp residues 222-416. Engineered: yes

Source:

Pediculus humanus subsp. Corporis. Body louse. Organism_taxid: 121224. Gene: phum_phum467460. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: phum_phum164330. Expression_system_taxid: 562

Resolution:

2.70Å R-factor: 0.184 R-free: 0.217

Authors:

B.Ren,T.S.Peat,V.A.Streltsov,M.Pollard,R.Fernley,J.Grusovin, S.Seabrook,P.Pilling,T.Phan,L.Lu,G.O.Lovrecz,L.D.Graham,R.J.Hill

Key ref:

B.Ren et al. (2014). Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits. Acta Crystallogr D Biol Crystallogr, 70, 1954-1964. PubMed id: 25004972 DOI: 10.1107/S1399004714009626

Date:

19-Feb-14 Release date: 30-Jul-14

Protein chain

E0VVT4  (E0VVT4_PEDHC) -  Ecdysone receptor from Pediculus humanus subsp. corporis

Seq: 520 a.a.

Struc: 238 a.a.*

Protein chain

E0VFQ5  (E0VFQ5_PEDHC) -  Retinoid X receptor, putative from Pediculus humanus subsp. corporis

Seq: 420 a.a.

Struc: 195 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains E, U: E.C.?

DOI no: 10.1107/S1399004714009626

Acta Crystallogr D Biol Crystallogr 70:1954-1964 (2014)

PubMed id: 25004972

Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits.

B.Ren, T.S.Peat, V.A.Streltsov, M.Pollard, R.Fernley, J.Grusovin, S.Seabrook, P.Pilling, T.Phan, L.Lu, G.O.Lovrecz, L.D.Graham, R.J.Hill.

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.