ArticleNature communications2024
Outer membrane protein assembly mediated by BAM-SurA complexes.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 2026Article
- Mechanistic basis of LolDF-mediated lipoprotein transport in Acinetobacter.Nature communications · 2026Article
- Article
- BAM-BepA complexes in outer membrane protein quality control.Nature communications · 2026Article
- L-type pyocins inhibit the BAM complex to kill without cell entry.Nature communications · 2026Article
- Monitoring Membrane Protein Folding Assisted by Insertases and Translocases Using AFM-Based Single-Molecule Force Spectroscopy.Chemical reviews · 2026Review
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Periplasmic crowding and peptidoglycan hydrolase activity as drivers of outer membrane vesiculation in Acinetobacter baumannii.Communications biology · 2026Article
- Breaking the outer membrane barrier: structure, targets, and antimicrobial strategies for Gram-negative bacteria.Frontiers in microbiology · 2026Review
- A fluorescent reporter and single-turnover kinetics reveal insight into BAM complex function.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.Journal of structural biology: X · 2025Article
- Loss of essential outer membrane functions causes drug hypersensitization inbioRxiv : the preprint server for biology · 2025Article
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- Article
- Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function.Nature communications · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Article
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The outer membrane is a formidable barrier that protects Gram-negative bacteria against environmental threats. Its integrity requires the correct folding and insertion of outer membrane proteins (OMPs) by the membrane-embedded β-barrel assembly machinery (BAM). Unfolded OMPs are delivered to BAM by the periplasmic chaperone SurA, but how SurA and BAM work together to ensure successful OMP delivery and folding remains unclear. Here, guided by AlphaFold2 models, we use disulphide bond engineering in an attempt to trap SurA in the act of OMP delivery to BAM, and solve cryoEM structures of a series of complexes. The results suggest that SurA binds BAM at its soluble POTRA-1 domain, which may trigger conformational changes in both BAM and SurA that enable transfer of the unfolded OMP to the BAM lateral gate for insertion into the outer membrane. Mutations that disrupt the interaction between BAM and SurA result in outer membrane assembly defects, supporting the key role of SurA in outer membrane biogenesis.
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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.