1n3g

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[[Image:1n3g.png|left|200px]]
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==Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli==
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<StructureSection load='1n3g' size='340' side='right' caption='[[1n3g]], [[NMR_Ensembles_of_Models | 29 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n3g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N3G FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n3g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n3g RCSB], [http://www.ebi.ac.uk/pdbsum/1n3g PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n3/1n3g_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_1n3g| PDB=1n3g | SCENE= }}
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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<ref>PMID:12470636</ref>
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===Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12470636}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1n3g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3G OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012470636</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Bayer, P.]]
[[Category: Bayer, P.]]

Revision as of 16:10, 28 September 2014

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

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