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

Schubeis T, Le Marchand T, Daday C, Kopec W, Movellan KT, Stanek J, Schwarzer TS, Castiglione K, de Groot BL, Pintacuda G, Andreas LB (2020)


Publication Type: Journal article

Publication year: 2020

Journal

Book Volume: 117

Pages Range: 21014-21021

Journal Issue: 35

DOI: 10.1073/pnas.2002598117

Abstract

The protein AlkL is known to increase permeability of the outer membrane of bacteria for hydrophobic molecules, yet the mechanism of transport has not been determined. Differing crystal and NMR structures of homologous proteins resulted in a controversy regarding the degree of structure and the role of long extracellular loops. Here we solve this controversy by determining the de novo NMR structure in near-native lipid bilayers, and by accessing structural dynamics relevant to hydrophobic substrate permeation through molecular-dynamics simulations and by characteristic NMR relaxation parameters. Dynamic lateral exit sites large enough to accommodate substrates such as carvone or octane occur through restructuring of a barrel extension formed by the extracellular loops.

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APA:

Schubeis, T., Le Marchand, T., Daday, C., Kopec, W., Movellan, K.T., Stanek, J.,... Andreas, L.B. (2020). A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL. Proceedings of the National Academy of Sciences of the United States of America, 117(35), 21014-21021. https://dx.doi.org/10.1073/pnas.2002598117

MLA:

Schubeis, Tobias, et al. "A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL." Proceedings of the National Academy of Sciences of the United States of America 117.35 (2020): 21014-21021.

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