2.1 A resolution refined structure of a TATA box-binding protein (TBP).
The three-dimensional structure of a TATA box-binding protein (TBP2) from Arabidopsis thaliana has been refined at 2.1 A resolution. TBPs are general eukaryotic transcription factors that participate in initiation of RNA synthesis by all three eukaryotic RNA polymerases. The carboxy-terminal portion of TBP is a unique DNA-binding motif/protein fold, adopting a highly symmetric alpha/beta structure that resembles a molecular saddle with two stirrup-like loops. A ten-stranded, antiparallel beta-sheet provides a concave surface for recognizing class II nuclear gene promoters, while the four amphipathic alpha-helices on the convex surface are available for interaction with other transcription factors. The myriad interactions of TBP2 with components of the transcription machinery are discussed.
Nikolov
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Laboratory of Molecular Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.
Burley
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D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000737:chemistry; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry*; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010944:Plants / Q000737:chemistry; D011392:Proline / Q000737:chemistry; D011487:Protein Conformation; D029701:Saccharomyces cerevisiae Proteins; D017386:Sequence Homology, Amino Acid; D012997:Solvents / Q000737:chemistry; D016385:TATA Box; D035181:TATA-Box Binding Protein; D015534:Trans-Activators / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry*; D015533:Transcriptional Activation
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C075582:SPT3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D012997:Solvents; D035181:TATA-Box Binding Protein; D015534:Trans-Activators; D014157:Transcription Factors; D011392:Proline; D012321:DNA-Directed RNA Polymerases