Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP from Escherichia coli.
Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP from Escherichia coli.
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DOI：
10.1107/s1744309113011937
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发表时间：
2013-06
期刊：
影响因子：
--
通讯作者：
Yanjie Hou;De-Feng Li;Da Cheng Wang
中科院分区：
文献类型：
--
作者：
Yanjie Hou;De-Feng Li;Da Cheng Wang
在大肠杆菌和肠道沙门氏菌中，双-（3 '-5'）-环二聚鸟苷一磷酸（c-di-GMP）是一种普遍存在的细菌第二信使分子，参与许多细胞过程，可以调节鞭毛运动速度并降低细胞游泳速度通过结合到PilZ含有蛋白质YcgR。在这里，结晶和初步的X-射线晶体学分析的YcgR与c-di-GMP的报告。晶体的衍射分辨率为2.3 nm，空间群为R3：H，晶胞参数a = B = 93.96，c = 109.61 nm。不对称单位似乎含有一个亚基，其马修斯系数为3.21（3）Da（-1）。本研究结果为用c-di-GMP解析YcgR的晶体结构，并从三维结构上揭示其结构与功能的关系提供了可靠的依据。
In Escherichia coli and Salmonella enterica, bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP), a ubiquitous bacterial second-messenger molecule that participates in many cellular processes, can regulate flagellar motor speed and reduce cell swimming velocity by binding to the PilZ-containing protein YcgR. Here, the crystallization and preliminary X-ray crystallographic analysis of YcgR with c-di-GMP are reported. The crystals diffracted to 2.3 Å resolution and belonged to space group R3:H, with unit-cell parameters a = b = 93.96, c = 109.61 Å. The asymmetric unit appeared to contain one subunit with a Matthews coefficient of 3.21 Å(3) Da(-1). The results reported here provide a sound basis for solving the crystal structure of YcgR with c-di-GMP and revealing its structure-function relationship based on the three-dimensional structure.