5J3R

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

Summary for 5J3R

• Entry DOI: 10.2210/pdb5j3r/pdb
• Descriptor: Monothiol glutaredoxin-6, FE2/S2 (INORGANIC) CLUSTER, GLUTATHIONE, ... (4 entities in total)
• Functional Keywords: glutaredoxin, iron-sulfur cluster, saccharomyces cerevisiae, oxidoreductase
• Biological source: Saccharomyces cerevisiae S288c
• Cellular location: Vacuole : Q12438
• Total number of polymer chains: 1
• Total formula weight: 23307.65

Authors

Abdalla, M.,Dai, Y.-N.,Chi, C.-B.,Cheng, W.,Cao, D.-D.,Zhou, K.,Ali, W.,Chen, Y.,Zhou, C.-Z. (deposition date: 2016-03-31, release date: 2016-10-19, Last modification date: 2023-11-08)

Primary citation

Abdalla, M.,Dai, Y.-N.,Chi, C.-B.,Cheng, W.,Cao, D.-D.,Zhou, K.,Ali, W.,Chen, Y.,Zhou, C.-Z.
Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione-coordinated [2Fe-2S] cluster
Acta Crystallogr.,Sect.F, 72:732-737, 2016

PubMed Abstract: 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.

PubMed: 27710937
DOI: 10.1107/S2053230X16013418

Experimental method

X-RAY DIFFRACTION (2.46 Å)