Solution structure of the cold-shock-like protein fromRickettsia rickettsii

Autor: Caleb D. Frost, Jonathan M. Koch, Melissa M. Mueller, Christopher T. Veldkamp, Paul G. House, Emily R. Lackner, Justin T. O'Rorke, Heather A. Heinen, Andrew M. Fuchs, Francis C. Peterson, David R. Graupner, Scott J. Schoeller, Kyle P. Gerarden
Rok vydání: 2012
Předmět:
Models
Molecular
animal structures
Rocky Mountain spotted fever
Molecular Sequence Data
Rickettsia rickettsii
Biophysics
Tick
Biochemistry
DNA-binding protein
Protein Structure
Secondary
Conserved sequence
03 medical and health sciences
Bacterial Proteins
Structural Biology
Genetics
medicine
Structural Communications
Amino Acid Sequence
Nuclear Magnetic Resonance
Biomolecular
Peptide sequence
Conserved Sequence
Protein Unfolding
030304 developmental biology
0303 health sciences
biology
Protein Stability
030302 biochemistry & molecular biology
bacterial infections and mycoses
Condensed Matter Physics
biology.organism_classification
medicine.disease
Virology
NMR
Protein Structure
Tertiary
3. Good health
embryonic structures
cold-shock domains
Cold Shock Proteins and Peptides
Unfolded protein response
bacteria
Thermodynamics
OB folds
human activities
Bacteria
Zdroj: Acta Crystallographica Section F
ISSN: 1744-3091
Popis: The solution structure of the cold-shock-like protein from R. rickettsii, the causative agent of Rocky Mountain spotted fever, is reported.
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.
Databáze: OpenAIRE
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