8IFO

Crystal structure of estrogen related receptor-gamma DNA binding domain complexed with Pla2g12b promoter

Summary for 8IFO

• Entry DOI: 10.2210/pdb8ifo/pdb
• Descriptor: Estrogen-related receptor gamma, DNA (5'-D(*GP*AP*GP*GP*AP*CP*AP*AP*AP*GP*GP*TP*GP*AP*AP*AP*C)-3'), DNA (5'-D(*GP*TP*TP*TP*CP*AP*CP*CP*TP*TP*TP*GP*TP*CP*CP*TP*C)-3'), ... (6 entities in total)
• Functional Keywords: nuclear receptor, err3, pla2g12b, dr1, transcription
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 7
• Total formula weight: 58138.44

Authors

Xu, T.,Zhen, X.,Liu, J. (deposition date: 2023-02-19, release date: 2023-03-29, Last modification date: 2024-05-01)

Primary citation

Zhen, X.,Gan, Q.,Qu, L.,Dong, Y.,Pan, C.,Liu, J.,Wang, N.,Xu, T.
ERR gamma-DBD undergoes dimerization and conformational rearrangement upon binding to the downstream site of the DR1 element.
Biochem.Biophys.Res.Commun., 656:16-22, 2023

PubMed Abstract: The estrogen-related receptor (ERR) family members are reported to bind DNA elements as either monomer or dimer. However, to date, only one solution NMR structure of ERRβ in complex with a half-site DNA element has been reported. To better understand the DNA regulation mechanism, we determined the crystal structure of ERRγ-DBD bound to a natural DR1 element in Pla2g12b promoter to 2.2 Å resolution. Combined with biochemical assays, we show that ERRγ acts as a dimer and the C-terminal extension region undergoes conformational rearrangement when binding to the downstream DR1 element. In addition, the T-box region on the dimerization interface exhibits unique main-chain conformation. Thus, our structure presents a novel dimer interface for NR binding on DR1 DNA and provides a molecular basis for understanding the homodimer organization of ERR on DR1 elements.

PubMed: 36944284
DOI: 10.1016/j.bbrc.2023.03.038

Experimental method

X-RAY DIFFRACTION (2.2 Å)