ArticleAngewandte Chemie (International ed. in English)2022
Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Biochemical characterisation supports a central role for Oep80 from Arabidopsis thaliana in chloroplastic β-barrel protein assembly.Communications biology · 2025Article
- Article
- Pulsed Dipolar EPR for Self-Limited Complexes of Oligonucleotides Studies.Biomolecules · 2024Article
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells.Angewandte Chemie (International ed. in English) · 2023Article
- Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- GdJournal of the American Chemical Society · 2023Article
- EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms.The journal of physical chemistry. B · 2022Review
- Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes.Angewandte Chemie (International ed. in English) · 2022Article
- Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy.Angewandte Chemie (International ed. in English) · 2022Article
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2 authors.
Funding
Abstract
The β-barrel assembly machinery (BAM) consisting of the central β-barrel BamA and four other lipoproteins mediates the folding of the majority of the outer membrane proteins. BamA is placed in an asymmetric bilayer and its lateral gate is suggested to be the functional hotspot. Here we used in situ pulsed electron-electron double resonance spectroscopy to characterize BamA in the native outer membrane. In the detergent micelles, the data is consistent with mainly an inward-open conformation of BamA. The native membrane considerably enhanced the conformational heterogeneity. The lateral gate and the extracellular loop 3 exist in an equilibrium between different conformations. The outer membrane provides a favorable environment for occupying multiple conformational states independent of the lipoproteins. Our results reveal a highly dynamic behavior of the lateral gate and other key structural elements and provide direct evidence for the conformational modulation of a membrane protein in situ.
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