Unknown

Dataset Information

0

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.

SUBMITTER: Banci L 

PROVIDER: S-EPMC3160886 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

altmetric image

Publications

In-cell NMR in E. coli to monitor maturation steps of hSOD1.

Banci Lucia L   Barbieri Letizia L   Bertini Ivano I   Cantini Francesca F   Luchinat Enrico E  

PloS one 20110824 8


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-  ...[more]

Similar Datasets

| S-EPMC7015911 | biostudies-literature
| S-EPMC3427097 | biostudies-literature
| S-EPMC5511039 | biostudies-literature
| S-EPMC7092720 | biostudies-literature
| S-EPMC6689974 | biostudies-literature
| S-EPMC5358835 | biostudies-literature
| S-EPMC1913287 | biostudies-literature
| S-EPMC7355412 | biostudies-literature
| S-EPMC6662845 | biostudies-literature
| S-EPMC10097672 | biostudies-literature