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
Hauptverfasser: Kim, J.L, Nikolov, D.B, Burley, S.K
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.
ISSN:0028-0836
1476-4687
DOI:10.1038/365520a0