Co-crystal structure of TBP recognizing the minor groove of a TATA element
The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 angstroms resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing...
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Veröffentlicht in: | Nature (London) 1993-10, Vol.365 (6446), p.520-527 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter has been determined by X-ray crystallography at 2.25 angstroms resolution. Binding of the saddle-shaped protein induces a conformational change in the DNA, inducing sharp kinks at either end of the sequence TATAAAAG. Between the kinks, the right-handed double helix is smoothly curved and partially unwound, presenting a widened minor groove to TBP's concave, antiparallel beta-sheet. Side-chain/base interactions are restricted to the minor groove, and include hydrogen bonds, van der Waals contacts and phenylalanine-base stacking interactions. |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/365520a0 |