CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF A TATA ELEMENT

被引:1017
作者
KIM, JL [1 ]
NIKOLOV, DB [1 ]
BURLEY, SK [1 ]
机构
[1] ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
关键词
D O I
10.1038/365520a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The three-dimensional structure of a TATA-box binding polypeptide complexed with the TATA element of the adenovirus major late promoter ha's been determined by X-ray crystallography at 2.25 angstrom 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.
引用
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页码:520 / 527
页数:8
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