1.9-ANGSTROM RESOLUTION REFINED STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF TATAAAAG

被引：210

作者：

KIM, JL ^{[1
]}

BURLEY, SK ^{[1
]}

机构：

[1] ROCKEFELLER UNIV,HOWARD HUGHES MED INST,MOLEC BIOPHYS LABS,NEW YORK,NY 10021

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 09期

关键词：

D O I：

10.1038/nsb0994-638

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The three-dimensional structure of a TATA box-binding protein (TBP) from Arabidopsis thaliana complexed with a fourteen base pair oligonucleotide bearing the Adenovirus major late promoter TATA element has been refined at 1.9 Angstrom resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped alpha/beta protein induces an unprecedented conformational change in the DNA. A detailed structural and functional analysis of this unusual protein-DNA complex is presented, with particular emphasis on the mechanisms of DNA deformation, TATA element recognition, and preinitiation complex assembly.

引用

页码：638 / 653

页数：16

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