2E7P
Crystal structure of the holo form of glutaredoxin C1 from populus tremula x tremuloides
Summary for 2E7P
| Entry DOI | 10.2210/pdb2e7p/pdb |
| Descriptor | Glutaredoxin, FE2/S2 (INORGANIC) CLUSTER, GLUTATHIONE, ... (4 entities in total) |
| Functional Keywords | thioredoxin fold, glutaredoxin, poplar, electron transport |
| Biological source | Populus tremula x Populus tremuloides |
| Total number of polymer chains | 4 |
| Total formula weight | 51145.88 |
| Authors | Unno, H.,Takahashi, T.,Kawakami, T.,Aimoto, S.,Hase, T.,Kusunoki, M.,Rouhier, N.,Jacquot, J.P. (deposition date: 2007-01-12, release date: 2007-09-25, Last modification date: 2024-03-13) |
| Primary citation | Rouhier, N.,Unno, H.,Bandyopadhyay, S.,Masip, L.,Kim, S.K.,Hirasawa, M.,Gualberto, J.M.,Lattard, V.,Kusunoki, M.,Knaff, D.B.,Georgiou, G.,Hase, T.,Johnson, M.K.,Jacquot, J.P. Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1 Proc.Natl.Acad.Sci.Usa, 104:7379-7384, 2007 Cited by PubMed Abstract: 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. PubMed: 17460036DOI: 10.1073/pnas.0702268104 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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