Structural highlights
2lyq is a 1 chain structure with sequence from "enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Related: | 2gzu, 1utx, 2xi8, 2xiu, 2xj3, 2lyj, 2lyk, 2lyl, 2lyp, 2lyr, 2lys |
| Gene: | cylR2 ("Enterococcus proteiformis" Thiercelin and Jouhaud 1903) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum |
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
