View source for 2lyl


==NOE-based 3D structure of the predissociated homodimer of CylR2 in equilibrium with monomer at 266K (-7 Celsius degrees)==
<StructureSection load='2lyl' size='340' side='right'caption='[[2lyl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lyl]] 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=2LYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LYL 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=2lyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lyl OCA], [https://pdbe.org/2lyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lyl RCSB], [https://www.ebi.ac.uk/pdbsum/2lyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lyl 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lyl" 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]]