Ferritin-like molecules show a remarkable combination of the evolutionary conserved activity of iron uptake and release that engage different pores in the conserved ferritin shell. It was hypothesized that pore selection and iron traffic depend on dynamic allostery with no conformational changes in the ferritin backbone. In this study, we develop a novel network-weaving algorithm1 (NWA) that passes threads of an allosteric network through highly correlated residues using hierarchical clustering. Applying NWA in conjunction with a packing-on elastic network model2we detect allosteric networks in four representative eukaryotic and prokaryotic ferritins and characterize their relationship to the iron translocation pathways. The results show that the allosteric networks engage species-specific pores and a ferroxidase center consistently with experimental observations of iron transport. The residue-residue correlations and the resultant structure of the allosteric networks depend significantly on the ferritin shell packing, which, in turn, depends on protein sequence composition. This relationship explains the diversity of iron pathways suggested by experimental approaches.1. A.M. Ruvinsky, I.A. Vakser, M. Rivera, J. Chem. Phys., 2014, in print.2. A.M. Ruvinsky, I.A. Vakser. J. Chem. Phys. 133, 155101, 2010.

Allosteric networks in ferritin-like molecules

248th National Meeting (2014)

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