3WSH

EDTA-treated, oxidized HcgD from Methanocaldococcus jannaschii

Summary for 3WSH

• Entry DOI: 10.2210/pdb3wsh/pdb
• Related: 3WSD 3WSE 3WSF 3WSG 3WSI
• Descriptor: Putative GTP cyclohydrolase 1 type 2, FE (III) ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: nif3-related protein, metal binding protein
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 12
• Total formula weight: 340877.53

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

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)