1TBP
CRYSTAL STRUCTURE OF YEAST TATA-BINDING PROTEIN AND MODEL FOR INTERACTION WITH DNA
1TBP の概要
| エントリーDOI | 10.2210/pdb1tbp/pdb |
| 分子名称 | TATA-BINDING PROTEIN (1 entity in total) |
| 機能のキーワード | binding protein |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
| 細胞内の位置 | Nucleus: P13393 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 40329.75 |
| 構造登録者 | Chasman, D.I.,Flaherty, K.M.,Sharp, P.A.,Kornberg, R.D. (登録日: 1993-08-02, 公開日: 1994-01-31, 最終更新日: 2024-02-14) |
| 主引用文献 | Chasman, D.I.,Flaherty, K.M.,Sharp, P.A.,Kornberg, R.D. Crystal structure of yeast TATA-binding protein and model for interaction with DNA. Proc.Natl.Acad.Sci.USA, 90:8174-8178, 1993 Cited by PubMed Abstract: The C-terminal 179-aa region of yeast (Saccharomyces cerevisiae) TATA-binding protein (TBP), phylogenetically conserved and sufficient for many functions, formed crystals diffracting to 1.7-A resolution. The structure of the protein, determined by molecular replacement with coordinates from Arabidopsis TBP and refined to 2.6 A, differed from that in Arabidopsis slightly by an angle of about 12 degrees between two structurally nearly identical subdomains, indicative of a degree of conformational flexibility. A model for TBP-DNA interaction is proposed with the following important features: the long dimension of the protein follows the trajectory of the minor groove; two rows of basic residues conserved between the subdomains lie along the edges of the protein in proximity to the DNA phosphates; a band of hydrophobic residues runs down the middle of the groove; and amino acid residues whose mutation alters specificity for the second base of the TATA sequence are juxtaposed to that base. PubMed: 8367480DOI: 10.1073/pnas.90.17.8174 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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