3WOA

Crystal structure of lambda repressor (1-45) fused with maltose-binding protein

Summary for 3WOA

• Entry DOI: 10.2210/pdb3woa/pdb
• Related PRD ID: PRD_900001
• Descriptor: Repressor protein CI, Maltose-binding periplasmic protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: lambda repressor, maltose-binding protein, dna binding protein, sugar binding protein
• Biological source: Enterobacteria phage lambda; More
• Total number of polymer chains: 1
• Total formula weight: 46258.33

Authors

Hanazono, Y.,Takeda, K.,Miki, K. (deposition date: 2013-12-25, release date: 2015-04-29, Last modification date: 2023-11-08)

Primary citation

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, 8:1312-1321, 2018

PubMed Abstract: Nascent polypeptide chains fold cotranslationally, but the atomic-level details of this process remain unknown. Here, we report crystallographic, modeling, and spectroscopic studies of intermediate-length variants of the λ 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 λ 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.

PubMed: 30087834
DOI: 10.1002/2211-5463.12480

Experimental method

X-RAY DIFFRACTION (2 Å)