1tbp
From Proteopedia
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CRYSTAL STRUCTURE OF YEAST TATA-BINDING PROTEIN AND MODEL FOR INTERACTION WITH DNA
Overview
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.
About this Structure
1TBP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast TATA-binding protein and model for interaction with DNA., Chasman DI, Flaherty KM, Sharp PA, Kornberg RD, Proc Natl Acad Sci U S A. 1993 Sep 1;90(17):8174-8. PMID:8367480
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