title: Crystal structure of TFIID TATA-box binding protein.
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.
authors.affiliation: Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021-6399.
authors.forename: D B
authors.initials: DB
authors.lastname: Nikolov
authors.forename: S H
authors.initials: SH
authors.lastname: Hu
authors.forename: J
authors.initials: J
authors.lastname: Lin
authors.forename: A
authors.initials: A
authors.lastname: Gasch
authors.forename: A
authors.initials: A
authors.lastname: Hoffmann
authors.forename: M
authors.initials: M
authors.lastname: Horikoshi
authors.forename: N H
authors.initials: NH
authors.lastname: Chua
authors.forename: R G
authors.initials: RG
authors.lastname: Roeder
authors.forename: S K
authors.initials: SK
authors.lastname: Burley
mesh_terms: 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
chemical_list: D035362:Transcription Factor TFIID; D014157:Transcription Factors; D004247:DNA