ArticleNature communications2018
Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Lateral gating mechanism and plasticity of the β-barrel assembly machinery complex in micelles andPNAS nexus · 2024Article
- Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes.Angewandte Chemie (International ed. in English) · 2022Article
- Production and Preparation of Isotopically Labeled Human Membrane Proteins in Pichia pastoris for Fast-MAS-NMR Analyses.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Metabolomics and health: from nutritional crops and plant-based pharmaceuticals to profiling of human biofluids.Cellular and molecular life sciences : CMLS · 2021Review
- Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy.Nature protocols · 2021Article
- Endogenous membrane stress induces T6SS activity inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Integrative modeling of membrane-associated protein assemblies.Nature communications · 2020Article
- Proton-Detected Solid-State NMR of the Cell-Free Synthesized α-Helical Transmembrane Protein NS4B from Hepatitis C Virus.Chembiochem : a European journal of chemical biology · 2020Article
- Multi-receiver solid-state NMR using polarization optimized experiments (POE) at ultrafast magic angle spinning.Journal of biomolecular NMR · 2020Article
- Magnetic Alignment of Polymer Nanodiscs Probed by Solid-State NMR Spectroscopy.Langmuir : the ACS journal of surfaces and colloids · 2020Article
- The big BAM theory: An open and closed case?Biochimica et biophysica acta. Biomembranes · 2020Review
- Use of paramagnetic systems to speed-up NMR data acquisition and for structural and dynamic studies.Solid state nuclear magnetic resonance · 2019Review
- Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel.Nature communications · 2019Article
- Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach.Journal of biomolecular NMR · 2019Article
- Review
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Authors and funding
6 authors at 1 institution in 3 countries.
Funding
Abstract
The β-barrel assembly machinery (BAM) is a pentameric complex (BamA-E), which catalyzes the essential process of β-barrel protein insertion into the outer membrane of E. coli. Thus far, a detailed understanding of the insertion mechanism has been elusive but recent results suggest that local protein motion, in addition to the surrounding membrane environment, may be of critical relevance. We have devised a high-sensitivity solid-state NMR approach to directly probe protein motion and the structural changes associated with BAM complex assembly in lipid bilayers. Our results reveal how essential BamA domains, such as the interface formed by the polypeptide transport associated domains P4 and P5 become stabilized after complex formation and suggest that BamA β-barrel opening and P5 reorientation is directly related to complex formation in membranes. Both the lateral gate, as well as P5, exhibit local dynamics, a property that could play an integral role in substrate recognition and insertion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.