Crystal structure of TFIID TATA-box binding protein

Abstract

The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDτ) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 Å resolution. This highly symmetric α/β structure contains a new DMA-binding fold, resembling a molecular 'saddle' that sits astride the DMA. The DNA-binding surface is a curved, antiparallel β-sheet. When bound to DMA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins. © 1992 Nature Publishing Group.