2lyk
From Proteopedia
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| - | + | ==NOE-based 3D structure of the CylR2 homodimer at 270K (-3 Celsius degrees)== | |
| - | + | <StructureSection load='2lyk' size='340' side='right' caption='[[2lyk]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2lyk]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LYK FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gzu|2gzu]], [[1utx|1utx]], [[2xi8|2xi8]], [[2xiu|2xiu]], [[2xj3|2xj3]], [[2lyj|2lyj]], [[2lyl|2lyl]], [[2lyp|2lyp]], [[2lyq|2lyq]], [[2lyr|2lyr]], [[2lys|2lys]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cylR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 Enterococcus faecalis])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lyk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lyk RCSB], [http://www.ebi.ac.uk/pdbsum/2lyk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
| - | [[Category: Becker, S | + | [[Category: Becker, S]] |
| - | [[Category: Cho, M | + | [[Category: Cho, M]] |
| - | [[Category: Giller, K | + | [[Category: Giller, K]] |
| - | [[Category: Jaremko, L | + | [[Category: Jaremko, L]] |
| - | [[Category: Jaremko, M | + | [[Category: Jaremko, M]] |
| - | [[Category: Kim, H | + | [[Category: Kim, H]] |
| - | [[Category: Schwieters, C D | + | [[Category: Schwieters, C D]] |
| - | [[Category: Zweckstetter, M | + | [[Category: Zweckstetter, M]] |
[[Category: Cold denaturation]] | [[Category: Cold denaturation]] | ||
[[Category: Cylr2]] | [[Category: Cylr2]] | ||
Revision as of 12:56, 18 December 2014
NOE-based 3D structure of the CylR2 homodimer at 270K (-3 Celsius degrees)
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