2LYQ
NOE-based 3D structure of the monomeric intermediate of CylR2 at 262K (-11 Celsius degrees)
Summary for 2LYQ
| Entry DOI | 10.2210/pdb2lyq/pdb |
| Related | 1UTX 2GZU 2LYJ 2LYK 2LYL 2LYP 2LYR 2LYS 2XI8 2XIU 2XJ3 |
| NMR Information | BMRB: 17896 |
| Descriptor | CylR2 (1 entity in total) |
| Functional Keywords | cylr2, dna binding protein, noe-based structure, protein folding, cold denaturation, cytolysin repressor 2, helix-turn-helix |
| Biological source | Enterococcus faecalis |
| Total number of polymer chains | 1 |
| Total formula weight | 7724.99 |
| Authors | Jaremko, M.,Jaremko, L.,Kim, H.,Cho, M.,Schwieters, C.D.,Giller, K.,Becker, S.,Zweckstetter, M. (deposition date: 2012-09-19, release date: 2013-02-20, Last modification date: 2024-05-15) |
| Primary citation | Jaremko, M.,Jaremko, L.,Kim, H.Y.,Cho, M.K.,Schwieters, C.D.,Giller, K.,Becker, S.,Zweckstetter, M. Cold denaturation of a protein dimer monitored at atomic resolution. Nat.Chem.Biol., 9:264-270, 2013 Cited by PubMed Abstract: 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 °C to -16 °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. PubMed: 23396077DOI: 10.1038/nchembio.1181 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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