3WSI
EDTA-treated, reduced HcgD from Methanocaldococcus jannaschii
Summary for 3WSI
Entry DOI | 10.2210/pdb3wsi/pdb |
Related | 3WSD 3WSE 3WSF 3WSG 3WSH |
Descriptor | Putative GTP cyclohydrolase 1 type 2, FE (II) ION, PHOSPHATE ION, ... (4 entities in total) |
Functional Keywords | nif3-related protein, metal binding protein |
Biological source | Methanocaldococcus jannaschii |
Total number of polymer chains | 6 |
Total formula weight | 170432.21 |
Authors | Fujishiro, T.,Ermler, U.,Shima, S. (deposition date: 2014-03-13, release date: 2014-08-27, Last modification date: 2023-11-08) |
Primary citation | Fujishiro, T.,Ermler, U.,Shima, S. A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis Febs Lett., 588:2789-2793, 2014 Cited by PubMed Abstract: HcgD, a homolog of the ubiquitous Nif3-like protein family, is found in a gene cluster involved in the biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase. The presented crystal structure and biochemical analyses indicated that HcgD has a dinuclear iron-center, which provides a pronounced binding site for anionic ligands. HcgD contains a stronger and a weaker bound iron; the latter being removable by chelating reagents preferentially in the oxidized state. Therefore, we propose HcgD as an iron chaperone in FeGP cofactor biosynthesis, which might also stimulate investigations on the functionally unknown but physiologically important eukaryotic Nif3-like protein family members. PubMed: 24931373DOI: 10.1016/j.febslet.2014.05.059 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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