Geiger J H, Hahn S, Lee S, Sigler P B
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06510, USA.
Science. 1996 May 10;272(5263):830-6. doi: 10.1126/science.272.5263.830.
The crystal structure of the yeast TFIIA/TBP/TATA promoter complex was solved to 3 angstrom resolution by double-edge multiple wavelength anomalous diffraction from two different species of anomalous scattering elements in the same crystal. The large and small subunits of TFIIA associate intimately to form both domains of a two-domain folding pattern. TFIIA binds as a heterodimer to the side of the TBP/TATA complex opposite to the side that binds TFIIB and does not alter the TBP/DNA interaction. The six-stranded beta-sandwich domain interacts with the amino-terminal end of TBP through a stereospecific parallel beta-strand interface and with the backbone of the TATA box and the 5'-flanking B-DNA segment. The four-helix-bundle domain projects away from the TBP/TATA complex, thereby presenting a substantial surface for further protein-protein interactions.
通过在同一晶体中来自两种不同种类异常散射元素的双边多波长异常衍射，将酵母TFIIA/TBP/TATA启动子复合物的晶体结构解析到3埃的分辨率。TFIIA的大亚基和小亚基紧密结合，形成两结构域折叠模式的两个结构域。TFIIA作为异二聚体结合到TBP/TATA复合物与结合TFIIB的一侧相对的一侧，且不改变TBP/DNA相互作用。六链β-折叠结构域通过立体特异性平行β-链界面与TBP的氨基末端相互作用，并与TATA框的主链和5'-侧翼B-DNA片段相互作用。四螺旋束结构域从TBP/TATA复合物中伸出，从而为进一步的蛋白质-蛋白质相互作用提供了一个可观的表面。
