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• W1976022528 abstract "The import of essential organometallic micronutrients (such as iron-siderophores and vitamin B(12)) across the outer membrane of Gram-negative bacteria proceeds via TonB-dependent outer membrane transporters (TBDTs). The TBDT couples to the TonB protein, which is part of a multiprotein complex in the plasma (inner) membrane. Five crystal structures of TBDTs illustrate clearly the architecture of the protein in energy-independent substrate-free and substrate-bound states. In each of the TBDT structures, an N-terminal hatch (or plug or cork) domain occludes the lumen of a 22-stranded beta barrel. The manner by which substrate passes through the transporter (the hatch-barrel problem) is currently unknown. Solution NMR and X-ray crystallographic structures of various TonB domains indicate a striking structural plasticity of this protein. Thermodynamic, biochemical and bacteriological studies of TonB and TBDTs indicate further that existing structures do not yet capture critical energy-dependent and in vivo conformations of the transport cycle. The reconciliation of structural and non-structural experimental data, and the unambiguous experimental elucidation of a detailed molecular mechanism of transport are current challenges for this field." @default.
• W1976022528 created "2016-06-24" @default.
• W1976022528 creator A5017063200 @default.
• W1976022528 date "2005-08-01" @default.
• W1976022528 modified "2023-09-30" @default.
• W1976022528 title "TonB-dependent outer membrane transport: going for Baroque?" @default.
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• W1976022528 doi "https://doi.org/10.1016/j.sbi.2005.07.001" @default.
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