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A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL

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Schubeis, Tobias | Le Marchand, Tanguy | Daday, Csaba | Kopec, Wojciech | Tekwani Movellan, Kumar | Stanek, Jan | Schwarzer, Tom, S | Castiglione, Kathrin | de Groot, Bert, L | Pintacuda, Guido | Andreas, Loren, B

Edité par CCSD ; National Academy of Sciences -

International audience. The protein AlkL is known to increase permeability of the outermembrane of bacteria for hydrophobic molecules, yet the mech-anism of transport has not been determined. Differing crystal andNMR structures of homologous proteins resulted in a controversyregarding the degree of structure and the role of long extracellularloops. Here we solve this controversy by determining the de novoNMR structure in near-native lipid bilayers, and by accessing struc-tural dynamics relevant to hydrophobic substrate permeationthrough molecular-dynamics simulations and by characteristicNMR relaxation parameters. Dynamic lateral exit sites large enoughto accommodate substrates such as carvone or octane occur throughrestructuring of a barrel extension formed by the extracellularloops

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