CRYSTAL-STRUCTURE OF THE DNA-BINDING DOMAIN OF THE HEAT-SHOCK TRANSCRIPTION FACTOR
CRYSTAL-STRUCTURE OF THE DNA-BINDING DOMAIN OF THE HEAT-SHOCK TRANSCRIPTION FACTOR
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DOI：
10.1126/science.8284672
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发表时间：
1994-01-14
期刊：
影响因子：
56.9
通讯作者：
NELSON, HCM
中科院分区：
文献类型：
--
作者：
HARRISON, CJ;BOHM, AA;NELSON, HCM
在1.8埃分辨率下测定的DNA结合结构域的结构包含由四链反平行β折叠封端的三螺旋束。这种结构是螺旋-转角-螺旋基序的变体，以分解代谢物激活蛋白为代表。在热休克转录因子中，基序的第一螺旋（α 2）具有α-螺旋凸起和脯氨酸诱导的扭结。基序的两个螺旋之间的角度（α 2和α 3）比典型的螺旋-转角-螺旋蛋白的平均值小约20度。然而，束的第一和第三螺旋（α 1和α 3）的相对位置是保守的。这里提出三螺旋束的第一螺旋被认为是螺旋-转角-螺旋基序的一个组成部分。
The structure of the DNA binding domain, determined at 1.8 angstrom resolution, contains a three-helix bundle that is capped by a four-stranded antiparallel beta sheet. This structure is a variant of the helix-turn-helix motif, typified by catabolite activator protein. In the heat shock transcription factor, the first helix of the motif (alpha2) has an alpha-helical bulge and a proline-induced kink. The angle between the two helices of the motif (alpha2 and alpha3) is about 20-degrees smaller than the average for canonical helix-turn-helix proteins. Nevertheless, the relative positions of the first and third helices of the bundle (alpha1 and alpha3) are conserved. It is proposed here that the first helix of the three-helix bundle be considered a component of the helix-turn-helix motif.