Structural highlights
Function
[RPC1_LAMBD] Repressor protein CI allows phage lambda to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein CI to the OR and OL operators, preventing transcription of proteins necessary for lytic development.
Publication Abstract from PubMed
Nascent polypeptide chains fold cotranslationally, but the atomic-level details of this process remain unknown. Here, we report crystallographic, de novo modeling, and spectroscopic studies of intermediate-length variants of the lambda repressor N-terminal domain. Although the ranges of helical regions of the half-length variant were almost identical to those of the full-length protein, the relative orientations of these helices in the intermediate-length variants differed. Our results suggest that cotranslational folding of the lambda repressor initially forms a helical structure with a transient conformation, as in the case of a molten globule state. This conformation subsequently matures during the course of protein synthesis. Database: Structural data are available in the PDB under the accession numbers http://www.rcsb.org/pdb/search/structidSearch.do?structureId=5ZCA and http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3WOA.
Co-translational folding of alpha-helical proteins: structural studies of intermediate-length variants of the lambda repressor.,Hanazono Y, Takeda K, Miki K FEBS Open Bio. 2018 Jun 27;8(8):1312-1321. doi: 10.1002/2211-5463.12480., eCollection 2018 Aug. PMID:30087834[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hanazono Y, Takeda K, Miki K. Co-translational folding of alpha-helical proteins: structural studies of intermediate-length variants of the lambda repressor. FEBS Open Bio. 2018 Jun 27;8(8):1312-1321. doi: 10.1002/2211-5463.12480., eCollection 2018 Aug. PMID:30087834 doi:http://dx.doi.org/10.1002/2211-5463.12480
