NMR spectroscopic study of a Glutaredoxin1 from Clostridium oremlandii

Grx1 is a thiol-disulfide oxidoreductase from gram positive bacterium Clostridium oremlandii(strain OhILAs), that plays a role in maintaining the cellular redox homeostasis. Here we report the protein purification and NMR spectroscopic study of recombinant Grx1 double mutant U13C/C16S. We collected 3D NMR spectra and assigned all the backbone chemical shifts including Cα, Cβ, CO, HN, and N of Grx1. The secondary structure estimated from chemical shifts shows that Grx1 protein is well folded and consists of three α-helices and four β-strands. This NMR result is very useful for further structural and functional study of Grx1 protein.