Skip to Main content Skip to Navigation
Journal articles

Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site

Abstract : Glutaredoxins are glutathione-dependent enzymes that function to reduce disulfide bonds in vivo. Interestingly, a recent discovery indicates that some glutaredoxins can also exist in another form, an iron-sulfur protein [Lillig, C. H., et al. (2005) Proc. Natl. Acad. Sci. U.S.A. 102, 8168-8173]. This provides a direct connection between glutaredoxins and iron-sulfur proteins, suggesting a possible new regulatory role of iron-sulfur clusters along with the new functional switch of glutaredoxins. Biochemical studies have indicated that poplar glutaredoxin C1 (Grx-C1) is also such a biform protein. The apo form (monomer) of Grx-C1 is a regular glutaredoxin, and the holo form (dimer) is an iron-sulfur protein with a bridging [2Fe-2S] cluster. Here, we report the structural characterizations of poplar Grx-C1 in both the apo and holo forms by NMR spectroscopy. The solution structure of the reduced apo Grx-C1, which is the first plant Grx structure, shows a typical Grx fold. When poplar Grx-C1 forms a dimer with an iron-sulfur cluster, each subunit of the holo form still retains the overall fold of the apo form. The bridging iron-sulfur cluster in holo Grx-C1 is coordinated near the active site. In addition to the iron-sulfur cluster linker, helix 3 of each subunit is probably involved in the direct contact between the two subunits. Moreover, two glutathione molecules are identified in the vicinity of the iron-sulfur cluster and very likely participate in cluster coordination. Taken together, we propose that the bridging [2Fe-2S] cluster is coordinated by the first cysteine at the glutaredoxin active site from each subunit of holo Grx-C1, along with two cysteines from two glutathione molecules. Our studies reveal that holo Grx-C1 has a novel structural and iron-sulfur cluster coordination pattern for an iron-sulfur protein.
Document type :
Journal articles
Complete list of metadata

https://hal.inrae.fr/hal-02655662
Contributor : Migration Prodinra Connect in order to contact the contributor
Submitted on : Friday, May 29, 2020 - 10:42:47 PM
Last modification on : Wednesday, September 8, 2021 - 4:02:08 PM

Links full text

Identifiers

Collections

Citation

Yingang Feng, Nan Zhong, Nicolas Rouhier, Toshiharu Hase, Masami Kusunoki, et al.. Structural insight into poplar glutaredoxin C1 with a bridging iron-sulfur cluster at the active site. Biochemistry, American Chemical Society, 2006, 45 (26), pp.7998-8008. ⟨10.1021/bi060444t⟩. ⟨hal-02655662⟩

Share

Metrics

Record views

26