1N3G

Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli

Summary for 1N3G

• Entry DOI: 10.2210/pdb1n3g/pdb
• NMR Information: BMRB: 5389
• Descriptor: Protein yfiA (1 entity in total)
• Functional Keywords: cold shock, translation inhibitor, dsrbd, translation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12803.58

Authors

Rak, A.,Kalinin, A.,Shcherbakov, D.,Bayer, P. (deposition date: 2002-10-28, release date: 2003-01-28, Last modification date: 2024-05-29)

Primary citation

Rak, A.,Kalinin, A.,Shcherbakov, D.,Bayer, P.
Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia col
Biochem.Biophys.Res.Commun., 299:710-714, 2002

PubMed 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.

PubMed: 12470636
DOI: 10.1016/S0006-291X(02)02721-3

Experimental method

SOLUTION NMR