2e7p
From Proteopedia
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Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides
Overview
When expressed in Escherichia coli, cytosolic poplar glutaredoxin C1 (CGYC, active site) exists as a dimeric iron-sulfur-containing holoprotein or as, a monomeric apoprotein in solution. Analytical and spectroscopic studies, of wild-type protein and site-directed variants and structural, characterization of the holoprotein by using x-ray crystallography, indicate that the holoprotein contains a subunit-bridging [2Fe-2S] cluster, that is ligated by the catalytic cysteines of two glutaredoxins and the, cysteines of two glutathiones. Mutagenesis data on a variety of poplar, glutaredoxins suggest that the incorporation of an iron-sulfur cluster, could be a general feature of plant glutaredoxins possessing a glycine, adjacent to the catalytic cysteine. In light of these results, the, possible involvement of plant glutaredoxins in oxidative stress sensing or, iron-sulfur biosynthesis is discussed with respect to their intracellular, localization.
About this Structure
2E7P is a Single protein structure of sequence from Populus tremula x populus tremuloides with and as ligands. Full crystallographic information is available from OCA.
Reference
Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1., Rouhier N, Unno H, Bandyopadhyay S, Masip L, Kim SK, Hirasawa M, Gualberto JM, Lattard V, Kusunoki M, Knaff DB, Georgiou G, Hase T, Johnson MK, Jacquot JP, Proc Natl Acad Sci U S A. 2007 May 1;104(18):7379-84. Epub 2007 Apr 25. PMID:17460036
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