Structural and Biochemical Characterization of Yeast Monothiol Glutaredoxin Grx6 |
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Authors: | Ming Luo Xiao-Xiao Ma Yong-Xing He Rong-Guang Zhang Cong-Zhao Zhou |
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Institution: | 1 Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, People's Republic of China 2 Structural Biology Center, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA |
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Abstract: | Glutaredoxins (Grxs) are a ubiquitous family of proteins that reduce disulfide bonds in substrate proteins using electrons from reduced glutathione (GSH). The yeast Saccharomyces cerevisiae Grx6 is a monothiol Grx that is localized in the endoplasmic reticulum and Golgi compartments. Grx6 consists of three segments, a putative signal peptide (M1-I36), an N-terminal domain (K37-T110), and a C-terminal Grx domain (K111-N231, designated Grx6C). Compared to the classic dithiol glutaredoxin Grx1, Grx6 has a lower glutathione disulfide reductase activity but a higher glutathione S-transferase activity. In addition, similar to human Grx2, Grx6 binds GSH via an iron-sulfur cluster in vitro. The N-terminal domain is essential for noncovalent dimerization, but not required for either of the above activities. The crystal structure of Grx6C at 1.5 Å resolution revealed a novel two-strand antiparallel β-sheet opposite the GSH binding groove. This extra β-sheet might also exist in yeast Grx7 and in a group of putative Grxs in lower organisms, suggesting that Grx6 might represent the first member of a novel Grx subfamily. |
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Keywords: | β-ME-SG glutathionylated β-mercaptoehanol Fe-S iron-sulfur GR glutathione reductase Grx glutaredoxin Grx6C C-terminal domain of Grx6 GSH reduced glutathione GSSG glutathione disulfide GST glutathione S-transferase HEDS bis-(2-hydroxyethyl)-disulfide NBD-Cl 4-chloro-7-nitro-2 1 3-benzoxadiazole PDB Protein Data Bank Trx thioredoxin |
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