Summary information and primary citation
- PDB-id
- 8ifo; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- transcription
- Method
- X-ray (2.2 Å)
- Summary
- Crystal structure of estrogen related receptor-gamma DNA binding domain complexed with pla2g12b promoter
- Reference
- Zhen X, Gan Q, Qu L, Dong Y, Pan C, Liu J, Wang N, Xu T (2023): "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. doi: 10.1016/j.bbrc.2023.03.038.
- 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.
