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

نویسندگان

  • 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
چکیده

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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عنوان ژورنال:

دوره 68  شماره 

صفحات  -

تاریخ انتشار 2012