色氨酸无辅阻遏物在1.8埃时的晶体结构表明了结合色氨酸是如何增强对DNA的亲和力的。
The crystal structure of trp aporepressor at 1.8 A shows how binding tryptophan enhances DNA affinity.
作者信息
Zhang R G, Joachimiak A, Lawson C L, Schevitz R W, Otwinowski Z, Sigler P B
出版信息
Nature. 1987;327(6123):591-7. doi: 10.1038/327591a0.
DOI:10.1038/327591a0
PMID:3600756
Abstract
Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs. These flexible 'DNA-reading heads' flank a highly inflexible core domain formed by an unusual arrangement of interlocking alpha-helices from both subunits.
摘要
无活性的未结合配体的色氨酸阻遏物与色氨酸阻遏蛋白的晶体结构比较表明，结合色氨酸通过移动两个对称排列的柔性双螺旋基序，使二聚体的活性提高了一千倍。这些柔性的“DNA阅读头”位于一个高度刚性的核心结构域两侧，该核心结构域由来自两个亚基的互锁α螺旋的异常排列形成。
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