Atomic-resolution monitoring of protein maturation in live human cells by NMR
Banci L., Barbieri L., Bertini I., Luchinat E., Secci E., Zhao Y., Aricescu AR.
We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment. © 2013 Nature America, Inc.