1TBP

CRYSTAL STRUCTURE OF YEAST TATA-BINDING PROTEIN AND MODEL FOR INTERACTION WITH DNA

Summary for 1TBP

• Entry DOI: 10.2210/pdb1tbp/pdb
• Descriptor: TATA-BINDING PROTEIN (1 entity in total)
• Functional Keywords: binding protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P13393
• Total number of polymer chains: 2
• Total formula weight: 40329.75

Authors

Chasman, D.I.,Flaherty, K.M.,Sharp, P.A.,Kornberg, R.D. (deposition date: 1993-08-02, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

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

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: 8367480
DOI: 10.1073/pnas.90.17.8174

Experimental method

X-RAY DIFFRACTION (2.6 Å)