期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 117, 期 35, 页码 21014-21021出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2002598117
关键词
membrane protein; lipid bilayers; protein structure; protein dynamics; magic-angle spinning
资金
- European Research Council [GA 648974]
- CNRS (IR-RMN) [FR3050]
- European Commission (Project iNext) [GA 653706]
- German Research Foundation [AN1316/1-1, SFB803, INST 186/794-3, FOR 2518]
- German Federal Ministry of Education and Research (BMBF) [GA 031A178]
- MSCA incoming fellowship [GA 661799]
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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