Gated pores in the ferritin protein nanocage
نویسندگان
چکیده
منابع مشابه
Peptides selected for the protein nanocage pores change the rate of iron recovery from the ferritin mineral.
Pores regulate access between ferric-oxy biomineral inside and reductants/chelators outside the ferritin protein nanocage to control iron demineralization rates. The pore helix/loop/helix motifs that are contributed by three subunits unfold independently of the protein cage, as observed by crystallography, Fe removal rates, and CD spectroscopy. Pore unfolding is induced in wild type ferritin by...
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Iron is concentrated in ferritin, a spherical protein with a capacious cavity for ferric nanominerals of <4,500 Fe atoms. Global ferritin structure is very stable, resisting 6 M urea and heat (85 degrees C) at neutral pH. Eight pores, each formed by six helices from 3 of the 24 polypeptide subunits, restrict mineral access to reductant, protons, or chelators. Protein-directed transport of Fe an...
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ژورنال
عنوان ژورنال: Inorganica Chimica Acta
سال: 2008
ISSN: 0020-1693
DOI: 10.1016/j.ica.2007.08.025