2lyj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NOE-based 3D structure of the CylR2 homodimer at 298K== | |
| + | <StructureSection load='2lyj' size='340' side='right'caption='[[2lyj]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lyj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LYJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LYJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lyj OCA], [https://pdbe.org/2lyj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lyj RCSB], [https://www.ebi.ac.uk/pdbsum/2lyj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lyj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q8VL32_ENTFL Q8VL32_ENTFL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2 at temperatures from 25 degrees C to -16 degrees C reveal a progressive dissociation of the dimeric protein into a native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding. | ||
| - | + | Cold denaturation of a protein dimer monitored at atomic resolution.,Jaremko M, Jaremko L, Kim HY, Cho MK, Schwieters CD, Giller K, Becker S, Zweckstetter M Nat Chem Biol. 2013 Feb 10. doi: 10.1038/nchembio.1181. PMID:23396077<ref>PMID:23396077</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2lyj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Enterococcus faecalis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Becker S]] | ||
| + | [[Category: Cho M]] | ||
| + | [[Category: Giller K]] | ||
| + | [[Category: Jaremko L]] | ||
| + | [[Category: Jaremko M]] | ||
| + | [[Category: Kim H]] | ||
| + | [[Category: Schwieters CD]] | ||
| + | [[Category: Zweckstetter M]] | ||
Current revision
NOE-based 3D structure of the CylR2 homodimer at 298K
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