Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione‐coordinated [2Fe–2S] cluster. Issue 10 (6th October 2016)

• Record Type: Journal Article
• Authors: Abdalla, Mohnad; Dai, Ya-Nan; Chi, Chang-Biao; Cheng, Wang; Cao, Dong-Dong; Zhou, Kang; Ali, Wafa; Chen, Yuxing; Zhou, Cong-Zhao
• Is Part Of: Acta crystallographica. Volume 72:Issue 10(2016:Oct.)
• Page Start: 732
• Page End: 737
• Publication Date: 2016-10-06
• Subjects: glutaredoxin -- iron–sulfur cluster -- Saccharomyces cerevisiae -- crystal structure -- oxidoreductase; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X16013418
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The dimeric structure of the C‐terminal domain of Grx6, bridged by one [2Fe–2S] cluster coordinated by the active‐site Cys136 and two external glutathione molecules, is reported. 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.