PMID:21887272
| Citation |
Banci, L, Barbieri, L, Bertini, I, Cantini, F and Luchinat, E (2011) In-cell NMR in E. coli to monitor maturation steps of hSOD1. PLoS ONE 6:e23561 |
|---|---|
| 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. |
| Links |
PubMed PMC3160886 Online version:10.1371/journal.pone.0023561 |
| Keywords |
Apoproteins/metabolism; Cell Extracts; Cysteine/metabolism; Cytoplasm/metabolism; Escherichia coli/metabolism; Humans; Magnetic Resonance Spectroscopy; Oxidation-Reduction; Protein Binding; Protein Denaturation; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Quaternary; Superoxide Dismutase/chemistry; Superoxide Dismutase/metabolism; Tryptophan/metabolism; Zinc/metabolism |
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