Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB
复制标题
DOI：
10.1016/s0092-8674(00)81914-5
复制
发表时间：
1997-03-07
期刊：
影响因子：
64.5
通讯作者：
Hakoshima, T
中科院分区：
文献类型：
--
作者：
Kato, M;Mizuno, T;Hakoshima, T
含组氨酸的磷酸转移结构域（HPt）是一种新型的蛋白质模块，具有活性组氨酸残基，在双组分信号系统中介导磷酸转移反应。已经提出了涉及HPt结构域的多步磷酸化中继用于这些信号传导途径。厌氧传感器激酶ArcB的HPt结构域的晶体结构已被确定在2.06埃分辨率。该结构域由六个α螺旋组成，其中包含四螺旋折叠。ArcB的HPt结构域和其他信号系统中的组件的序列相似性的模式可以解释的三维结构的光，并支持的结论，即HPt结构域具有共同的结构基序在原核生物和真核生物。
The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined at 2.06 Angstrom resolution. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes.