3woa

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

spinqualitylabelsall models 3woa, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3woa is a 1 chain structure with sequence from Escherichia coli K-12 and Escherichia virus Lambda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: GLC, PRD_900001 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.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 https://www.rcsb.org/pdb/search/structidSearch.do?structureId=5ZCA and https://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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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