立克次体冷冲击样蛋白的溶液结构。

Kyle P Gerarden, Andrew M Fuchs, Jonathan M Koch, Melissa M Mueller, David R Graupner, Justin T O'Rorke, Caleb D Frost, Heather A Heinen, Emily R Lackner, Scott J Schoeller, Paul G House, Francis C Peterson, Christopher T Veldkamp
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引用次数: 4

摘要

落基山斑疹热是由立克次体感染引起的。立克次体可通过受感染的硬体伊蚊科蜱的叮咬传播给包括人类在内的哺乳动物。鉴于立克次体基因组中仅含有一种冷休克样蛋白,并考虑到其他细菌中冷休克蛋白的基本性质,本文对立克次体中冷休克样蛋白的结构进行了研究。除了在β-链3和4之间发现一个短的α-螺旋外,立克次氏体冷冲击样蛋白的溶液结构具有典型的希腊键五链β-桶结构,在大多数冷冲击域中发现。此外,立克次体冷休克样蛋白的ΔG展开度为18.4 kJ mol(-1),与其他细菌冷休克蛋白相比具有相似的稳定性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Solution structure of the cold-shock-like protein from Rickettsia rickettsii.

Rocky Mountain spotted fever is caused by Rickettsia rickettsii infection. R. rickettsii can be transmitted to mammals, including humans, through the bite of an infected hard-bodied tick of the family Ixodidae. Since the R. rickettsii genome contains only one cold-shock-like protein and given the essential nature of cold-shock proteins in other bacteria, the structure of the cold-shock-like protein from R. rickettsii was investigated. With the exception of a short α-helix found between β-strands 3 and 4, the solution structure of the R. rickettsii cold-shock-like protein has the typical Greek-key five-stranded β-barrel structure found in most cold-shock domains. Additionally, the R. rickettsii cold-shock-like protein, with a ΔG of unfolding of 18.4 kJ mol(-1), has a similar stability when compared with other bacterial cold-shock proteins.

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期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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