CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR-GROOVE OF A TATA ELEMENT
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KIM, JL
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ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USAROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
KIM, JL
[1
]
NIKOLOV, DB
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ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USAROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
NIKOLOV, DB
[1
]
BURLEY, SK
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ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USAROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
BURLEY, SK
[1
]
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[1] ROCKEFELLER UNIV, MOLEC BIOPHYS LABS, 1230 YORK AVE, NEW YORK, NY 10021 USA
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.