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立氏立克次体冷休克样蛋白的溶液结构

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

作者信息

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

机构信息

Department of Chemistry, University of Wisconsin-Whitewater, 800 West Main Street, Whitewater, WI 53190, USA.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1284-8. doi: 10.1107/S174430911203881X. Epub 2012 Oct 26.

Abstract

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.

摘要

落基山斑疹热由立氏立克次体感染引起。立氏立克次体可通过感染的硬蜱科蜱虫叮咬传播给包括人类在内的哺乳动物。鉴于立氏立克次体基因组仅包含一种类冷休克蛋白,且考虑到冷休克蛋白在其他细菌中的重要性质,对立氏立克次体类冷休克蛋白的结构进行了研究。除了在β链3和4之间发现的一个短α螺旋外,立氏立克次体类冷休克蛋白的溶液结构具有大多数冷休克结构域中典型的希腊钥匙五链β桶结构。此外,立氏立克次体类冷休克蛋白的解折叠ΔG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。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f797/3515365/3a87ed400613/f-68-01284-fig1.jpg

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