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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
- Source :
- Journal of the American Chemical Society, Journal of the American Chemical Society, 2023, ⟨10.1021/jacs.2c10484⟩
- Publication Year :
- 2023
- Publisher :
- HAL CCSD, 2023.
-
Abstract
- International audience; 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.
Details
- Language :
- English
- ISSN :
- 00027863 and 15205126
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society, Journal of the American Chemical Society, 2023, ⟨10.1021/jacs.2c10484⟩
- Accession number :
- edsair.doi.dedup.....bfca7afc2eef31a7338894da2d5708d1