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The genome from Epstein–Barr virus (EBV) encodes for a class Ia ribonucleotide-reductase (RNR) small subunit (R2; BaRF1), which has a glutamate (Glu61) in the equivalent position of a metal-coordinating aspartate common to most R2s. We solved crystal structures of EBV R2 in metal-free, monometal, and diferrous states. Upon Fe2+ binding in the dimetal-binding site we observe a conformational disorder-to-order transition of the metal-coordinating Glu61 and two amino-acid segments in helices αB and α2/αD. Disorder as in EBV R2 exists for corresponding regions in structures of Homo sapiens p53-inducable R2 (p53R2) and in several other R2 orthologues. Thus the disorder-to-order transition represents a general phenomenon in R2s. Our data indicate differential affinities for iron in the dimetal site of EBV R2.
| Authors: | Florian Schmitzberger; Daniel Gurmu; Sue-Li Dahlroth; Pär Nordlund | |
| Journal: | ACS Chemical Biology | |
| Year: | 2012 | |
| DOI: | 10.1021/cb300098t | |
| Publication date: | 23-07-2012 |
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