2eff
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Crystal structure analysis of the complex between CyaY and Co(II)
OverviewOverview
Deficiency of the small mitochondrial protein frataxin causes Friedreich's, ataxia, a severe neurodegenerative pathology. Frataxin, which has been, highly conserved throughout evolution, is thought to be involved in, among, other processes, Fe-S cluster formation. Independent evidence shows that, it binds iron directly, although with very distinct features and low, affinity. Here, we have carried out an extensive study of the binding, properties of CyaY, the bacterial ortholog of frataxin, to different, divalent and trivalent cations, using NMR and X-ray crystallography. We, demonstrate that the protein has low cation specificity and contains, multiple binding sites able to chelate divalent and trivalent metals with, low affinity. Binding does not involve cavities or pockets, but exposed, glutamates and aspartates, which are residues that are unusual for iron, chelation when not assisted by histidines and/or cysteines. We have, related how such an ability to bind cations on a relatively large area, through an electrostatic mechanism could be a valuable asset for protein, function.
About this StructureAbout this Structure
2EFF is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Understanding the binding properties of an unusual metal-binding protein--a study of bacterial frataxin., Pastore C, Franzese M, Sica F, Temussi P, Pastore A, FEBS J. 2007 Aug;274(16):4199-210. Epub 2007 Jul 25. PMID:17651435
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