1TBA
SOLUTION STRUCTURE OF A TBP-TAFII230 COMPLEX: PROTEIN MIMICRY OF THE MINOR GROOVE SURFACE OF THE TATA BOX UNWOUND BY TBP, NMR, 25 STRUCTURES
Summary for 1TBA
Entry DOI | 10.2210/pdb1tba/pdb |
NMR Information | BMRB: 4223 |
Descriptor | TRANSCRIPTION INITIATION FACTOR IID 230K CHAIN, TRANSCRIPTION INITIATION FACTOR TFIID (2 entities in total) |
Functional Keywords | complex (transcription factors), tbp, taf, tafii230, tfiid, solution structure |
Biological source | Drosophila melanogaster (fruit fly) More |
Cellular location | Nucleus: P51123 P13393 |
Total number of polymer chains | 2 |
Total formula weight | 27133.43 |
Authors | Liu, D.,Ishima, R.,Tong, K.I.,Bagby, S.,Kokubo, T.,Muhandiram, D.R.,Kay, L.E.,Nakatani, Y.,Ikura, M. (deposition date: 1998-08-16, release date: 1999-08-16, Last modification date: 2024-05-22) |
Primary citation | Liu, D.,Ishima, R.,Tong, K.I.,Bagby, S.,Kokubo, T.,Muhandiram, D.R.,Kay, L.E.,Nakatani, Y.,Ikura, M. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell(Cambridge,Mass.), 94:573-583, 1998 Cited by PubMed Abstract: General transcription factor TFIID consists of TATA box-binding protein (TBP) and TBP-associated factors (TAF(II)s), which together play a central role in both positive and negative regulation of transcription. The N-terminal region of the 230 kDa Drosophila TAF(II) (dTAF(II)230) binds directly to TBP and inhibits TBP binding to the TATA box. We report here the solution structure of the complex formed by dTAF(II)230 N-terminal region (residues 11-77) and TBP. dTAF(II)230(11-77) comprises three alpha helices and a beta hairpin, forming a core that occupies the concave DNA-binding surface of TBP. The TBP-binding surface of dTAF(II)230 markedly resembles the minor groove surface of the partially unwound TATA box in the TBP-TATA complex. This protein mimicry of the TATA element surface provides the structural basis of the mechanism by which dTAF(II)230 negatively controls the TATA box-binding activity within the TFIID complex. PubMed: 9741622DOI: 10.1016/S0092-8674(00)81599-8 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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