Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved atp-binding cassette protein abce1*

HIGHLIGHTS

• who: Uma Sinha-Datta from the served extra cysteine within the, terminal Fe-S cluster domain, which can rescue Cys, (position, ) by ligand swappingThis extra cysteine, absent in most Archaea, explains why the mutation at position , (C S) in S. solfataricus , showed no assembled Fe-S clusters. Noteworthy, mutation of Cys, (extra cysteine) has no effect on , function in yeast. It is therefore questionable if ligand swapping occurs in vivo. ABC-type proteins are evolutionarily highly conserved molecular machines, coupling ATP binding and hydrolysis to conformational changes (43, ). The smallest functional unit appears to be an ABC . . .
  

   

  

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