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.
Nikolov
D B
DB
Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021-6399.
Hu
S H
SH
Lin
J
J
Gasch
A
A
Hoffmann
A
A
Horikoshi
M
M
Chua
N H
NH
Roeder
R G
RG
Burley
S K
SK
D000595:Amino Acid Sequence; D017360:Arabidopsis; D003198:Computer Simulation; D004247:DNA / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011401:Promoter Regions, Genetic / Q000502:physiology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D016385:TATA Box / Q000502:physiology; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000737:chemistry*; D015533:Transcriptional Activation / Q000502:physiology; D014961:X-Ray Diffraction
D035362:Transcription Factor TFIID; D014157:Transcription Factors; D004247:DNA