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Crystal structure of yeast monothiol glutaredoxin Grx6 in complex with a glutathione‐coordinated [2Fe–2S] cluster
Author(s) -
Abdalla Mohnad,
Dai Ya-Nan,
Chi Chang-Biao,
Cheng Wang,
Cao Dong-Dong,
Zhou Kang,
Ali Wafa,
Chen Yuxing,
Zhou Cong-Zhao
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16013418
Subject(s) - glutaredoxin , yeast , cluster (spacecraft) , glutathione , chemistry , crystal structure , crystal (programming language) , biochemistry , crystallography , enzyme , computer science , programming language
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.