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Zinc-containing ferredoxin from Acidianus ambivalens

A small protein from a hot-spring archaeon with seven iron atoms in two clusters, plus a zinc, all intact.

The ferredoxin (pale) with its [3Fe-4S] and [4Fe-4S] clusters (iron in brown, sulfur in yellow) held by cysteines (orange), and its zinc (grey) held by three histidines and an aspartate (plum).

Ferredoxins are small proteins that ferry electrons around the cell. This one comes from Acidianus ambivalens, an archaeon that lives in hot, acidic volcanic springs. It carries seven iron atoms in two iron–sulfur clusters, a [3Fe-4S] and a [4Fe-4S], and it also binds a zinc. An earlier structure of a related ferredoxin had its clusters converted artificially; here both clusters and the zinc site are intact, just as the organism makes them, at 2.0 Å resolution (paper).

It’s also one of the first proteins I crystallised. I grew the crystals at ITQB around 2000, between my undergraduate project and my PhD. They diffracted to 2.0 Å but were twinned, each with a different twinning ratio, so the structure took a long time to solve and refine. In the end the biochemistry caught up, it was important to get the structure out, and it was published in 2008.

PDB entry
2VKR at PDBe (also at RCSB PDB)
Released
2008-03-04
Resolution
2.01 Å
Paper
Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+) -containing ferredoxin. (FEBS Lett., 2008)
More
Technical details, links and electron density

Pictures and video rendered with UCSF ChimeraX; the 3D view is PDBe Mol*.

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