Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2LSS

Solution structure of the R. rickettsii cold shock-like protein

Summary for 2LSS
Entry DOI10.2210/pdb2lss/pdb
NMR InformationBMRB: 18442
DescriptorCold shock-like protein (1 entity in total)
Functional Keywordscold shock-like protein, csd, csp, oligonucleotide binding fold, ob fold, rna binding protein, dna binding protein
Biological sourceRickettsia rickettsii
Cellular locationCytoplasm (By similarity): A8GT84
Total number of polymer chains1
Total formula weight7781.74
Authors
Veldkamp, C.T.,Peterson, F.C.,Gerarden, K.P.,Fuchs, A.M.,Koch, J.M.,Mueller, M.M. (deposition date: 2012-05-04, release date: 2012-05-16, Last modification date: 2024-05-15)
Primary citationGerarden, K.P.,Fuchs, A.M.,Koch, J.M.,Mueller, M.M.,Graupner, D.R.,O'Rorke, J.T.,Frost, C.D.,Heinen, H.A.,Lackner, E.R.,Schoeller, S.J.,House, P.G.,Peterson, F.C.,Veldkamp, C.T.
Solution structure of the cold-shock-like protein from Rickettsia rickettsii.
Acta Crystallogr.,Sect.F, 68:1284-1288, 2012
Cited by
PubMed 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.
PubMed: 23143233
DOI: 10.1107/S174430911203881X
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227111

數據於2024-11-06公開中

PDB statisticsPDBj update infoContact PDBjnumon