Magic-angle spinning NMR structure of Opa60 in lipid bilayers
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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2024-06-01
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| Series: | Journal of Structural Biology: X |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590152424000035 |
| _version_ | 1797279270627704832 |
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| author | Marcel C. Forster Kumar Tekwani Movellan Eszter E. Najbauer Stefan Becker Loren B. Andreas |
| author_facet | Marcel C. Forster Kumar Tekwani Movellan Eszter E. Najbauer Stefan Becker Loren B. Andreas |
| author_sort | Marcel C. Forster |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-07T16:22:51Z |
| format | Article |
| id | doaj.art-9b5ab73b4868401ca4f03f07d442897b |
| institution | Directory Open Access Journal |
| issn | 2590-1524 |
| language | English |
| last_indexed | 2024-03-07T16:22:51Z |
| publishDate | 2024-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Structural Biology: X |
| spelling | doaj.art-9b5ab73b4868401ca4f03f07d442897b2024-03-04T04:12:20ZengElsevierJournal of Structural Biology: X2590-15242024-06-019100098Magic-angle spinning NMR structure of Opa60 in lipid bilayersMarcel C. Forster0Kumar Tekwani Movellan1Eszter E. Najbauer2Stefan Becker3Loren B. Andreas4Department of NMR-based Structural Biology, Max-Planck-Institute for Multidisciplinary Sciences, Am Faßberg 11, 37077 Göttingen, GermanyDepartment of NMR-based Structural Biology, Max-Planck-Institute for Multidisciplinary Sciences, Am Faßberg 11, 37077 Göttingen, GermanyDepartment of NMR-based Structural Biology, Max-Planck-Institute for Multidisciplinary Sciences, Am Faßberg 11, 37077 Göttingen, GermanyDepartment of NMR-based Structural Biology, Max-Planck-Institute for Multidisciplinary Sciences, Am Faßberg 11, 37077 Göttingen, GermanyCorresponding author.; Department of NMR-based Structural Biology, Max-Planck-Institute for Multidisciplinary Sciences, Am Faßberg 11, 37077 Göttingen, GermanyHere 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.http://www.sciencedirect.com/science/article/pii/S2590152424000035Solid-state NMRMembrane proteinMagic-angle spinningOpacity associated proteinAtomic resolution structure |
| spellingShingle | Marcel C. Forster Kumar Tekwani Movellan Eszter E. Najbauer Stefan Becker Loren B. Andreas Magic-angle spinning NMR structure of Opa60 in lipid bilayers Journal of Structural Biology: X Solid-state NMR Membrane protein Magic-angle spinning Opacity associated protein Atomic resolution structure |
| title | Magic-angle spinning NMR structure of Opa60 in lipid bilayers |
| title_full | Magic-angle spinning NMR structure of Opa60 in lipid bilayers |
| title_fullStr | Magic-angle spinning NMR structure of Opa60 in lipid bilayers |
| title_full_unstemmed | Magic-angle spinning NMR structure of Opa60 in lipid bilayers |
| title_short | Magic-angle spinning NMR structure of Opa60 in lipid bilayers |
| title_sort | magic angle spinning nmr structure of opa60 in lipid bilayers |
| topic | Solid-state NMR Membrane protein Magic-angle spinning Opacity associated protein Atomic resolution structure |
| url | http://www.sciencedirect.com/science/article/pii/S2590152424000035 |
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