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Solution structure of the ribosome-associated cold shock response protein Yfia of <i>Escherichia coli</i>

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons98720

Rak,  Alexey
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98678

Bayer,  Peter
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Rak, A., Kalinin, A., Shcherbakov, D., & Bayer, P. (2002). Solution structure of the ribosome-associated cold shock response protein Yfia of <i>Escherichia coli</i>. Biochemical and Biophysical Research Communications, 299(5): 1, pp. 710-714. Retrieved from http://dx.doi.org/10.1016/S0006-291X(02)02721-3.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-0D93-A
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 0.6 Angstrom. 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. (C) 2002 Elsevier Science (USA). All rights reserved.