Crystal structure of TFIID TATA-box binding protein
Copyright policy )Crystal structure of TFIID TATA-box binding protein
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.
- St Vincents Institute of Medical Research Australia
- University of California System United States
- Rockefeller University United States
- Howard Hughes Medical Institute United States
- University of Southern California United States
Models, Molecular, Transcriptional Activation, Molecular Structure, Sequence Homology, Amino Acid, Molecular Sequence Data, Arabidopsis, Molecular Conformation, DNA, TATA Box, X-Ray Diffraction, Computer Simulation, Transcription Factor TFIID, Amino Acid Sequence, Promoter Regions, Genetic, Sequence Alignment, Transcription Factors
Models, Molecular, Transcriptional Activation, Molecular Structure, Sequence Homology, Amino Acid, Molecular Sequence Data, Arabidopsis, Molecular Conformation, DNA, TATA Box, X-Ray Diffraction, Computer Simulation, Transcription Factor TFIID, Amino Acid Sequence, Promoter Regions, Genetic, Sequence Alignment, Transcription Factors
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