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鼠伤寒沙门氏菌冷休克蛋白E的结晶及X射线结构

Crystallization and X-ray structure of cold-shock protein E from Salmonella typhimurium.

作者信息

Morgan Hugh P, Wear Martin A, McNae Iain, Gallagher Maurice P, Walkinshaw Malcolm D

机构信息

Centre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, Edinburgh EH9 3JR, Scotland.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt 12):1240-5. doi: 10.1107/S1744309109033788. Epub 2009 Nov 27.

DOI:10.1107/S1744309109033788
PMID:20054119
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2802871/
Abstract

In prokaryotic organisms, cold shock triggers the production of a small highly conserved family of cold-shock proteins (CSPs). CSPs have been well studied structurally and functionally in Escherichia coli and Bacillus subtilis, but Salmonella typhimurium CSPs remain relatively uncharacterized. In S. typhimurium, six homologous CSPs have been identified: StCspA-E and StCspH. The crystal structure of cold-shock protein E from S. typhimurium (StCspE) has been determined at 1.1 A resolution and has an R factor of 0.203 after refinement. The three-dimensional structure is similar to those of previously determined CSPs and is composed of five antiparallel beta-strands forming a classic OB fold/five-stranded beta-barrel. This first structure of a CSP from S. typhimurium provides new insight into the cold-shock response of this bacterium.

摘要

在原核生物中，冷休克会触发一小类高度保守的冷休克蛋白（CSPs）的产生。CSPs在大肠杆菌和枯草芽孢杆菌中已得到充分的结构和功能研究，但鼠伤寒沙门氏菌的CSPs仍相对缺乏特征描述。在鼠伤寒沙门氏菌中，已鉴定出六种同源CSPs：StCspA - E和StCspH。鼠伤寒沙门氏菌冷休克蛋白E（StCspE）的晶体结构已在1.1埃分辨率下确定，精修后R因子为0.203。其三维结构与先前确定的CSPs相似，由五条反平行β链组成经典的OB折叠/五链β桶。鼠伤寒沙门氏菌CSPs的首个结构为该细菌的冷休克反应提供了新的见解。

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