Quantification of the Allosterically-Driven Unfolding of BtuB’s N-terminus upon B12 Binding by HDX-MS

Adam Maciej Zmyslowski
To import large metabolites across the outer membrane (OM) of Gram-negative bacteria, TonB dependent transporters (TBDTs) undergo significant conformational change. After substrate binding in BtuB, the E. coli vitamin B12 TBDT, TonB binds and couples BtuB to the inner membrane proton motive force which powers transport. The role of TonB in rearranging the plug domain to form a putative pore remains enigmatic. The aim of my thesis is to advance understanding of the substrate transport...
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