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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 es...

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Detalles Bibliográficos
Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3515365/
https://www.ncbi.nlm.nih.gov/pubmed/23143233
http://dx.doi.org/10.1107/S174430911203881X
Descripción
Sumario: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.