Crystal structure of TFIID TATA-box binding protein.

Nikolov, D B; Hu, S H; Lin, J; Gasch, A; Hoffmann, A; Horikoshi, M; Chua, N H; Roeder, R G et al. · Nature · 1992

basic_science · Level V

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Abstract

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

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