Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe – 2S] cluster

Glutaredoxins (Grxs) constitute a superfamily of proteins that perform diverse biological functions. The Saccharomyces cerevisiae glutaredoxin Grx6 not only serves as a glutathione (GSH)-dependent oxidoreductase and as a GSH transferase, but also as an essential [2Fe – 2S]-binding protein. Here, the dimeric structure of the C-terminal domain of Grx6 (holo Grx6C), bridged by one [2Fe – 2S] cluster coordinated by the active-site Cys136 and two external GSH molecules, is reported. Structural comparison combined with multiple-sequence alignment demonstrated that holo Grx6C is similar to the [2Fe – 2S] cluster-incorporated dithiol Grxs, which share a highly conserved [2Fe – 2S] cluster-binding pattern and dimeric conformation that is distinct from the previously identified [2Fe – 2S] cluster-ligated monothiol Grxs.

Source: Acta Crystallographica Section F - September 21, 2016 Category: Biochemistry Authors: Abdalla, M. Dai, Y.-N. Chi, C.-B. Cheng, W. Cao, D.-D. Zhou, K. Ali, W. Chen, Y. Zhou, C.-Z. Tags: glutaredoxin iron – sulfur cluster Saccharomyces cerevisiae crystal structure oxidoreductase research communications Source Type: research