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energy transducer TonB
The TonB_C domain is the well-characterised C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane [1]. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance [2]. [1]. 16741124. Outer membrane active transport: structure of the BtuB:TonB complex. Shultis DD, Purdy MD, Banchs CN, Wiener MC;. Science. 2006;312:1396-1399. [2]. 21277822. Recent insights into iron import by bacteria. Braun V, Hantke K;. Curr Opin Chem Biol. 2011;15:328-334. (from Pfam)
energy transducer TonB interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.)
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