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

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• 作者：Mohnad Abdalla ; Ya-Nan Dai ; Chang-Biao Chi ; Wang Cheng ; Dong-Dong Cao ; Kang Zhou ; Wafa Ali ; Yuxing Chen and Cong-Zhao Zhou
• 关键词：glutaredoxin ; iron&ndash ; sulfur cluster ; Saccharomyces cerevisiae ; crystal structure ; oxidoreductase
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：72
• 期：10
• 页码：732-737
• 全文大小：1412K
• ISSN：1744-3091

文摘

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.