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3WSI

EDTA-treated, reduced HcgD from Methanocaldococcus jannaschii

Summary for 3WSI
Entry DOI10.2210/pdb3wsi/pdb
Related3WSD 3WSE 3WSF 3WSG 3WSH
DescriptorPutative GTP cyclohydrolase 1 type 2, FE (II) ION, PHOSPHATE ION, ... (4 entities in total)
Functional Keywordsnif3-related protein, metal binding protein
Biological sourceMethanocaldococcus jannaschii
Total number of polymer chains6
Total formula weight170432.21
Authors
Fujishiro, T.,Ermler, U.,Shima, S. (deposition date: 2014-03-13, release date: 2014-08-27, Last modification date: 2023-11-08)
Primary citationFujishiro, 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: 24931373
DOI: 10.1016/j.febslet.2014.05.059
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

226707

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