Work

Crystal structure of yeast TATA-binding protein and model for interaction with DNA.

Year: 1993

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.90.17.8174

Authors: D I Chasman, K M Flaherty, P A Sharp, R D Kornberg

Institutions: Massachusetts Institute of Technology, Stanford University

Language: English

Topic: Genomics and Chromatin Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Cancer Institute, National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases

Awards: Structure of the Eukaryote Transcription Apparatus, Characterization of Pathways Controlling Cancer at the Level of Gene Regulation, G578988982, G986685044