Reference: Luo M, et al. (2010) Structural and biochemical characterization of yeast monothiol glutaredoxin Grx6. J Mol Biol 398(4):614-22

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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, like 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 A resolution revealed a novel two-strand antiparallel beta-sheet at the opposite of the GSH binding groove. This extra beta-sheet might also exist in yeast Grx7, and a group of putative Grxs in lower organisms, suggesting that Grx6 might represent the first member of a novel Grx subfamily.CI - Copyright (c) 2010. Published by Elsevier Ltd.

Reference Type
Journal Article
Authors
Luo M, Jiang YL, Ma XX, Tang YJ, He YX, Yu J, Zhang RG, Chen Y, Zhou CZ
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