Nolte R T, Conlin R M, Harrison S C, Brown R S
Harvard Medical School, Boston, MA 02115, USA.
Proc Natl Acad Sci U S A. 1998 Mar 17;95(6):2938-43. doi: 10.1073/pnas.95.6.2938.
The crystal structure of the six NH2-terminal zinc fingers of Xenopus laevis transcription factor IIIA (TFIIIA) bound with 31 bp of the 5S rRNA gene promoter has been determined at 3.1 A resolution. Individual zinc fingers are positioned differently in the major groove and across the minor groove of DNA to span the entire length of the duplex. These results show how TFIIIA can recognize several separated DNA sequences by using fewer fingers than necessary for continuous winding in the major groove.
非洲爪蟾转录因子IIIA(TFIIIA)的六个氨基末端锌指与5S rRNA基因启动子的31个碱基对结合的晶体结构已在3.1埃分辨率下确定。各个锌指在DNA的大沟和小沟中的定位不同,以跨越双链体的整个长度。这些结果表明了TFIIIA如何通过使用比在大沟中连续缠绕所需的手指更少的手指来识别几个分开的DNA序列。