Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus.
Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus.
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DOI：
10.1016/j.jinorgbio.2005.12.001
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发表时间：
2006-05
影响因子：
3.9
通讯作者：
Bradley D. Ramsay;B. Wiedenheft;M. Allen;G. Gauss;C. Lawrence;M. Young;T. Douglas
中科院分区：
文献类型：
--
作者：
Bradley D. Ramsay;B. Wiedenheft;M. Allen;G. Gauss;C. Lawrence;M. Young;T. Douglas
Oxidative stress is a universal phenomenon experienced by organisms in all domains of life. Proteins like those in the ferritin-like di-iron carboxylate superfamily have evolved to manage this stress. Here we describe the cloning, isolation, and characterization of a Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus (PfDps-like). Phylogenetic analysis, primary structure alignments and higher order structural predictions all suggest that the P. furiosus protein is related to proteins within the broad superfamily of ferritin-like di-iron carboxylate proteins. The recombinant PfDps protein self-assembles into a 12 subunit quaternary structure with an outer shell diameter of ∼10nm and an interior diameter of ∼5nm. Dps proteins functionally manage the toxicity of oxidative stress by sequestering intracellular ferrous iron and using it to reduce H2O2in a two electron process to form water. The iron is converted to a benign form as Fe(III) within the protein cage. This Dps-mediated reduction of hydrogen peroxide, coupled with the protein’s capacity to sequester iron, contributes to its service as a multifunctional antioxidant.
