title: In-cell NMR in E. coli to monitor maturation steps of hSOD1.
abstract: In-cell NMR allows characterizing the folding state of a protein as well as posttranslational events at molecular level, in the cellular context. Here, the initial maturation steps of human copper, zinc superoxide dismutase 1 are characterized in the E. coli cytoplasm by in-cell NMR: from the apo protein, which is partially unfolded, to the zinc binding which causes its final quaternary structure. The protein selectively binds only one zinc ion, whereas in vitro also the copper site binds a non-physiological zinc ion. However, no intramolecular disulfide bridge formation occurs, nor copper uptake, suggesting the need of a specific chaperone for those purposes.
authors: Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy. banci@cerm.unifi.it
authors: Lucia
authors: L
authors: Banci
authors: Letizia
authors: L
authors: Barbieri
authors: Ivano
authors: I
authors: Bertini
authors: Francesca
authors: F
authors: Cantini
authors: Enrico
authors: E
authors: Luchinat
mesh_terms: D001059:Apoproteins / Q000378:metabolism; D002457:Cell Extracts; D003545:Cysteine / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D020836:Protein Structure, Quaternary; D013482:Superoxide Dismutase / Q000737:chemistry / Q000378:metabolism*; D000072105:Superoxide Dismutase-1; D014364:Tryptophan / Q000378:metabolism; D015032:Zinc / Q000378:metabolism
chemical_list: D001059:Apoproteins; D002457:Cell Extracts; C000606290:SOD1 protein, human; D014364:Tryptophan; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1; D015032:Zinc; D003545:Cysteine