3L4N

Crystal structure of yeast monothiol glutaredoxin Grx6

Summary for 3L4N

• Entry DOI: 10.2210/pdb3l4n/pdb
• Descriptor: Monothiol glutaredoxin-6, GLUTATHIONE (3 entities in total)
• Functional Keywords: c-terminal domain of grx6, oxidoreductase
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Vacuole: Q12438
• Total number of polymer chains: 1
• Total formula weight: 15061.81

Authors

Luo, M.,Jiang, Y.-L.,Ma, X.-X.,He, Y.-X.,Tang, Y.-J.,Yu, J.,Zhang, R.-G.,Chen, Y.,Zhou, C.-Z. (deposition date: 2009-12-21, release date: 2010-04-07, Last modification date: 2011-12-14)

Primary citation

Luo, M.,Jiang, Y.-L.,Ma, X.-X.,Tang, Y.-J.,He, Y.-X.,Yu, J.,Zhang, R.-G.,Chen, Y.,Zhou, C.-Z.
Structural and biochemical characterization of yeast monothiol glutaredoxin Grx6
J.Mol.Biol., 398:614-622, 2010

PubMed 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 A resolution revealed a novel two-strand antiparallel beta-sheet opposite the GSH binding groove. This extra beta-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.

PubMed: 20347849
DOI: 10.1016/j.jmb.2010.03.029

Experimental method

X-RAY DIFFRACTION (1.5 Å)