来自大肠杆菌的GnsA的晶体结构。

Crystal structure of GnsA from Escherichia coli.

作者信息

Wei Yong, Zhan Lihong, Gao Zengqiang, Privé Gilbert G, Dong Yuhui

机构信息

School of Life Science, University of Science and Technology of China, Hefei 230027, China; Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.

School of Life Science, University of Science and Technology of China, Hefei 230027, China; Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.

出版信息

Biochem Biophys Res Commun. 2015 Jun 19;462(1):1-7. doi: 10.1016/j.bbrc.2015.03.133. Epub 2015 Apr 1.

DOI:10.1016/j.bbrc.2015.03.133

PMID:25839658

Abstract

Escherichia Coli GnsA is a regulator of phosphatidylethanolamine synthesis and functions as a suppressor of both a secG null mutation and fabA6 mutations. GnsA may also be a toxin with the cognate antitoxin YmcE. Here we report the crystal structure of GnsA to 1.8 Å. GnsA forms a V shaped hairpin structure that is tightly associated into a homodimer. Our comprehensive structural study suggests that GnsA is structurally similar to an outer membrane protein, suggesting a function of protein binding.

摘要

大肠杆菌GnsA是磷脂酰乙醇胺合成的调节因子，可作为secG无效突变和fabA6突变的抑制因子发挥作用。GnsA也可能是一种与同源抗毒素YmcE相关的毒素。在此，我们报告了分辨率为1.8 Å的GnsA晶体结构。GnsA形成一个V形发夹结构，紧密结合形成同源二聚体。我们全面的结构研究表明，GnsA在结构上与一种外膜蛋白相似，提示其具有蛋白质结合功能。