1VOK
ARABIDOPSIS THALIANA TBP (DIMER)
Summary for 1VOK
| Entry DOI | 10.2210/pdb1vok/pdb |
| Descriptor | TATA-BOX-BINDING PROTEIN, SULFATE ION (3 entities in total) |
| Functional Keywords | transcription initiation, dna binding, transcription factor |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 44896.77 |
| Authors | Nikolov, D.B.,Burley, S.K. (deposition date: 1996-04-29, release date: 1996-11-08, Last modification date: 2024-02-14) |
| Primary citation | Nikolov, D.B.,Burley, S.K. 2.1 A resolution refined structure of a TATA box-binding protein (TBP). Nat.Struct.Biol., 1:621-637, 1994 Cited by PubMed Abstract: 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. PubMed: 7634102DOI: 10.1038/nsb0994-621 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
