2lyk
From Proteopedia
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- | [[Image:2lyk.jpg|left|200px]] | ||
- | + | ==NOE-based 3D structure of the CylR2 homodimer at 270K (-3 Celsius degrees)== | |
+ | <StructureSection load='2lyk' size='340' side='right'caption='[[2lyk]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2lyk]] 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=2LYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LYK 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=2lyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lyk OCA], [https://pdbe.org/2lyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lyk RCSB], [https://www.ebi.ac.uk/pdbsum/2lyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lyk 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 2lyk" style="background-color:#fffaf0;"></div> | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
- | [[Category: Becker | + | [[Category: Large Structures]] |
- | [[Category: Cho | + | [[Category: Becker S]] |
- | [[Category: Giller | + | [[Category: Cho M]] |
- | [[Category: Jaremko | + | [[Category: Giller K]] |
- | [[Category: Jaremko | + | [[Category: Jaremko L]] |
- | [[Category: Kim | + | [[Category: Jaremko M]] |
- | [[Category: Schwieters | + | [[Category: Kim H]] |
- | [[Category: Zweckstetter | + | [[Category: Schwieters CD]] |
- | + | [[Category: Zweckstetter M]] | |
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Current revision
NOE-based 3D structure of the CylR2 homodimer at 270K (-3 Celsius degrees)
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