PMID:12470636

Citation	Rak, A, Kalinin, A, Shcherbakov, D and Bayer, P (2002) Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli. Biochem. Biophys. Res. Commun. 299:710-4
Abstract	The solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli was determined by nuclear magnetic resonance with a RMSD of 0.6A. Yfia shows a global beta-alpha-beta-beta-beta-alpha folding topology similar to its homologue HI0257 of Haemophilus influenzae and the double-strand-binding domain of Drosophila Staufen protein. Yfia and HI0257 differ in their surface charges and in the composition of their flexible C-termini, indicating their specificity to different target molecules. Both proteins exhibit a hydrophobic and polar region, which probably functions as interaction site for protein complex formation. Despite their similarity to the dsRBD fold, Yfia does not bind to model fragments of 16S ribosomal RNA as determined by NMR titration and gel shift experiments.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins; Cold Temperature; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; RNA/metabolism; RNA-Binding Proteins/chemistry; Ribosomal Proteins/chemistry; Ribosomal Proteins/metabolism; Sequence Homology, Amino Acid
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