一种新型厌氧传感器激酶ArcB的C端传递器HPt结构域与趋化反应调节因子CheY之间复合物的结晶。

Crystallization of a complex between a novel C-terminal transmitter, HPt domain, of the anaerobic sensor kinase ArcB and the chemotaxis response regulator CheY.

作者信息

Kato M, Mizuno T, Hakoshima T

机构信息

Department of Molecular Biology, Nara Institute of Science and Technology (NAIST), 8916-5 Takayama, Ikoma, Nara 630-01, Japan.

出版信息

Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):140-2. doi: 10.1107/s0907444997007075.

DOI:10.1107/s0907444997007075

PMID:9761838

Abstract

The histidine-containing phosphotransfer (HPt) domain at the C-terminus of the anaerobic sensor kinase ArcB has been cocrystallized with the chemotaxis response regulator CheY by a hanging-drop vapor-diffusion method. Crystals belong to space group P212121 with unit-cell dimensions a = 55.32, b = 76.29 and c = 83.89 A, with one molecule in the crystallographic asymmetric unit. The crystals diffract to 2.7 A resolution. This is the first crystallization of a protein-protein complex formed by a transmitter domain of sensor kinase and a receiver domain of response regulator in the two-component signal-transduction system.

摘要

厌氧传感器激酶ArcB C末端含组氨酸的磷酸转移（HPt）结构域已通过悬滴气相扩散法与趋化反应调节蛋白CheY共结晶。晶体属于空间群P212121，晶胞参数a = 55.32、b = 76.29和c = 83.89 Å，晶胞不对称单元中有一个分子。晶体衍射分辨率达2.7 Å。这是双组分信号转导系统中由传感器激酶的传递结构域和反应调节蛋白的接收结构域形成的蛋白质-蛋白质复合物的首次结晶。