Solution structure of the cold-shock-like protein from Rickettsia rickettsii.
Solution structure of the cold-shock-like protein from Rickettsia rickettsii.
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立克次体冷休克样蛋白的溶液结构。
DOI:
10.1107/s174430911203881x
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发表时间:
2012
期刊:
影响因子:
--
通讯作者:
Veldkamp,ChristopherT
中科院分区:
文献类型:
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作者:
Gerarden,KyleP;Fuchs,AndrewM;Koch,JonathanM;Mueller,MelissaM;Graupner,DavidR;O'Rorke,JustinT;Frost,CalebD;Heinen,HeatherA;Lackner,EmilyR;Schoeller,ScottJ;House,PaulG;Peterson,FrancisC;Veldkamp,ChristopherT
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.