3wsf

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Oxidized HcgD from Methanocaldococcus jannaschii with citrateOxidized HcgD from Methanocaldococcus jannaschii with citrate

Structural highlights

3wsf is a 6 chain structure with sequence from Methanocaldococcus jannaschii DSM 2661. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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.

A possible iron delivery function of the dinuclear iron center of HcgD in [Fe]-hydrogenase cofactor biosynthesis.,Fujishiro T, Ermler U, Shima S FEBS Lett. 2014 Aug 25;588(17):2789-93. doi: 10.1016/j.febslet.2014.05.059. Epub , 2014 Jun 12. PMID:24931373[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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. 2014 Aug 25;588(17):2789-93. doi: 10.1016/j.febslet.2014.05.059. Epub , 2014 Jun 12. PMID:24931373 doi:http://dx.doi.org/10.1016/j.febslet.2014.05.059

3wsf, resolution 2.00Å

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OCA