1n3g
From Proteopedia
(New page: 200px<br /><applet load="1n3g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n3g" /> '''Solution structure of the ribosome-associate...) |
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'''Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli'''<br /> | '''Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of the ribosome-associated cold shock response | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1N3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1N3G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: translation inhibitor]] | [[Category: translation inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:48 2008'' |
Revision as of 12:01, 21 February 2008
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Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli
Overview
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.
About this Structure
1N3G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli., Rak A, Kalinin A, Shcherbakov D, Bayer P, Biochem Biophys Res Commun. 2002 Dec 20;299(5):710-4. PMID:12470636
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