CRYSTAL-STRUCTURE OF TFIID TATA-BOX BINDING-PROTEIN

被引:358
作者
NIKOLOV, DB
HU, SH
LIN, J
GASCH, A
HOFFMANN, A
HORIKOSHI, M
CHUA, NH
ROEDER, RG
BURLEY, SK
机构
[1] ROCKEFELLER UNIV,MOLEC BIOPHYS LABS,1230 YORK AVE,NEW YORK,NY 10021
[2] ROCKEFELLER UNIV,PLANT MOLEC BIOL LAB,NEW YORK,NY 10021
[3] ROCKEFELLER UNIV,BIOCHEM & MOLEC BIOL LAB,NEW YORK,NY 10021
[4] ROCKEFELLER UNIV,HOWARD HUGHES MED INST,NEW YORK,NY 10021
关键词
D O I
10.1038/360040a0
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 structure of a central component of the eukaryotic transcriptional apparatus, a TATA-box binding protein (TBP or TFIIDtau) from Arabidopsis thaliana, has been determined by X-ray crystallography at 2.6 angstrom resolution. This highly symmetric alpha/beta structure contains a new DNA-binding fold, resembling a molecular 'saddle' that sits astride the DNA. The DNA-binding surface is a curved, antiparallel beta-sheet. When bound to DNA, the convex surface of the saddle would be presented for interaction with other transcription initiation factors and regulatory proteins.
引用
收藏
页码:40 / 46
页数:7
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