Magic-angle spinning NMR structure of Opa60 in lipid bilayers

Forster, Marcel C.; Tekwani Movellan, Kumar; Najbauer, Eszter É.; Becker, Stefan; Andreas, Loren B.

doi:10.1016/j.yjsbx.2024.100098

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学術論文

Magic-angle spinning NMR structure of Opa60 in lipid bilayers

MPS-Authors

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Forster, Marcel C.
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Tekwani Movellan, Kumar
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Najbauer, Eszter É.
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Becker, Stefan
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Andreas, Loren B.
Research Group of Solid State NMR Spectroscopy-2, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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1-s2.0-S2590152424000035-main.pdf
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引用

Forster, M. C., Tekwani Movellan, K., Najbauer, E. É., Becker, S., & Andreas, L. B. (2024). Magic-angle spinning NMR structure of Opa60 in lipid bilayers. Journal of Structural Biology: X, 9:. doi:10.1016/j.yjsbx.2024.100098.

引用: https://hdl.handle.net/21.11116/0000-000F-0E96-9

要旨

Here we report the structure of Opa60 in lipid bilayers using proton-detected magic-angle spinning nuclear magnetic resonance (MAS NMR). Preparations including near-native oligosaccharide lipids reveal a consistent picture of a stable transmembrane beta barrel with a minor increase in the structured region as compared with the previously reported detergent structure. The large variable loops known to interact with host proteins could not be detected, confirming their dynamic nature even in a lipid bilayer environment. The structure provides a starting point for investigation of the functional role of Opa60 in gonococcal infection, which is understood to involve interaction with host proteins. At the same time, it demonstrates the recent advances in proton-detected methodology for membrane protein structure determination at atomic resolution by MAS NMR.