PDBsum entry 2lyp

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protein links
DNA binding protein PDB id
Protein chain
66 a.a.
PDB id:
Name: DNA binding protein
Title: Noe-based 3d structure of the monomer of cylr2 in equilibriu predissociated homodimer at 266k (-7 celsius degrees)
Structure: Cylr2. Chain: a. Synonym: putative transcription regulator. Engineered: yes
Source: Enterococcus faecalis. Organism_taxid: 1351. Gene: cylr2. Expressed in: escherichia coli. Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: M.Jaremko,L.Jaremko,H.Kim,M.Cho,C.D.Schwieters,K.Giller,S.Be M.Zweckstetter
Key ref: M.Jaremko et al. (2013). Cold denaturation of a protein dimer monitored at atomic resolution. Nat Chem Biol, 9, 264-270. PubMed id: 23396077 DOI: 10.1038/nchembio.1181
19-Sep-12     Release date:   20-Feb-13    
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Protein chain
Pfam   ArchSchema ?
Q8VL32  (Q8VL32_ENTFL) -  CylR2
66 a.a.
66 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     DNA binding     2 terms  


DOI no: 10.1038/nchembio.1181 Nat Chem Biol 9:264-270 (2013)
PubMed id: 23396077  
Cold denaturation of a protein dimer monitored at atomic resolution.
M.Jaremko, ..Jaremko, H.Y.Kim, M.K.Cho, C.D.Schwieters, K.Giller, S.Becker, M.Zweckstetter.
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.