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. 1992 Nov 5;360(6399):40-6.
doi: 10.1038/360040a0.

Crystal structure of TFIID TATA-box binding protein

D B Nikolov  1 , S H Hu, J Lin, A Gasch, A Hoffmann, M Horikoshi, N H Chua, R G Roeder, S K Burley
Affiliations

Crystal structure of TFIID TATA-box binding protein

D B Nikolov et al. Nature. .

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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