Crystal structure of TFIID TATA-box binding protein
- 1 November 1992
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 360 (6399) , 40-46
- https://doi.org/10.1038/360040a0
Abstract
The structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDtau) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 angstrom 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.Keywords
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