1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG

Joseph L. Kim; Stephen K. Burley

doi:10.1038/nsb0994-638

1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG

Joseph L. Kim, Stephen K. Burley

Research output: Contribution to journal › Article › peer-review

200 Scopus citations

Abstract

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 Å resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped α/β 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.

Original language	English (US)
Pages (from-to)	638-653
Number of pages	16
Journal	Nature Structural Biology
Volume	1
Issue number	9
DOIs	https://doi.org/10.1038/nsb0994-638
State	Published - Sep 1994
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Genetics

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10.1038/nsb0994-638

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abstract = "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 {\AA} resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped α/β 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.",

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AB - 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 Å resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped α/β 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.

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1.9 Å resolution refined structure of TBP recognizing the minor groove of TATAAAAG

Abstract

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