Evidence for [2Fe-2S] 2+ and Linear [3Fe-4S] 1+ Clusters in a Unique Family of Glycine/Cysteine-Rich Fe-S Proteins from Megavirinae Giant Viruses - Archive ouverte HAL Access content directly
Journal Articles Journal of the American Chemical Society Year : 2023

Evidence for [2Fe-2S] 2+ and Linear [3Fe-4S] 1+ Clusters in a Unique Family of Glycine/Cysteine-Rich Fe-S Proteins from Megavirinae Giant Viruses

Abstract

We have discovered a protein with an amino acid composition exceptionally rich in glycine and cysteine residues in the giant virus mimivirus. This small 6 kDa protein is among the most abundant proteins in the icosahedral 0.75 μm viral particles; it has no predicted function but is probably essential for infection. The aerobically purified red-brownish protein overproduced inEscherichia coli contained both iron and inorganic sulfide. UV/vis, EPR, and Mössbauer studies revealed that the viral protein, coined GciS, accommodated two distinct Fe-S clusters: a diamagnetic S = 0 [2Fe-2S]2+ cluster and a paramagnetic S = 5/2 linear [3Fe-4S]1+ cluster, a geometry rarely stabilized in native proteins. Orthologs of mimivirus GciS were identified within all clades of Megavirinae, a Mimiviridae subfamily infecting Acanthamoeba, including the distantly related tupanviruses, and displayed the same spectroscopic features. Thus, these glycine/cysteine-rich proteins form a new family of viral Fe-S proteins sharing unique Fe-S cluster binding properties.

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Virology
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hal-03967087 , version 1 (01-02-2023)

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Alejandro Villalta, Batoul Srour, Audrey Lartigue, Martin Clémancey, Deborah Byrne, et al.. Evidence for [2Fe-2S] 2+ and Linear [3Fe-4S] 1+ Clusters in a Unique Family of Glycine/Cysteine-Rich Fe-S Proteins from Megavirinae Giant Viruses. Journal of the American Chemical Society, 2023, 145 (5), pp.2733-2738. ⟨10.1021/jacs.2c10484⟩. ⟨hal-03967087⟩
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