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| | ==NOE-based 3D structure of the CylR2 homodimer at 270K (-3 Celsius degrees)== | | ==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=''> | + | <StructureSection load='2lyk' size='340' side='right'caption='[[2lyk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lyk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. 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> | + | <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='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> | + | </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='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 proteiformis" Thiercelin and Jouhaud 1903])</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> |
| - | <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://pdbe.org/2lyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lyk RCSB], [http://www.ebi.ac.uk/pdbsum/2lyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lyk ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8VL32_ENTFL Q8VL32_ENTFL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Enterococcus faecalis]] |
| - | [[Category: Becker, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Cho, M]] | + | [[Category: Becker S]] |
| - | [[Category: Giller, K]] | + | [[Category: Cho M]] |
| - | [[Category: Jaremko, L]] | + | [[Category: Giller K]] |
| - | [[Category: Jaremko, M]] | + | [[Category: Jaremko L]] |
| - | [[Category: Kim, H]] | + | [[Category: Jaremko M]] |
| - | [[Category: Schwieters, C D]] | + | [[Category: Kim H]] |
| - | [[Category: Zweckstetter, M]] | + | [[Category: Schwieters CD]] |
| - | [[Category: Cold denaturation]]
| + | [[Category: Zweckstetter M]] |
| - | [[Category: Cylr2]]
| + | |
| - | [[Category: Cytolysin repressor 2]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Homodimer]]
| + | |
| - | [[Category: Noe-based structure]]
| + | |
| - | [[Category: Protein folding]]
| + | |
| Structural highlights
Function
Q8VL32_ENTFL
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jaremko M, Jaremko L, Kim HY, Cho MK, Schwieters CD, Giller K, Becker S, Zweckstetter M. Cold denaturation of a protein dimer monitored at atomic resolution. Nat Chem Biol. 2013 Feb 10. doi: 10.1038/nchembio.1181. PMID:23396077 doi:http://dx.doi.org/10.1038/nchembio.1181
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