ArticleBiochemistry2018
Folding Determinants of Transmembrane β-Barrels Using Engineered OMP Chimeras.
Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed.
- The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Evolutionary Engineering a Larger Porin Using a Loop-to-Hairpin Mechanism.Journal of molecular biology · 2023Article
- Evolutionary engineering a larger porin using a loop-to-hairpin mechanism.bioRxiv : the preprint server for biology · 2023Article
- Engineering a HyperstableJournal of the American Chemical Society · 2022Article
- Outer membrane protein evolution.Current opinion in structural biology · 2021Review
- Design, Screening, and Testing of Non-Rational Peptide Libraries with Antimicrobial Activity: In Silico and Experimental Approaches.Antibiotics (Basel, Switzerland) · 2020Review
- Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.The Journal of biological chemistry · 2020Review
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Transmembrane β-barrel proteins (OMPs) are highly robust structures for engineering and development of nanopore channels, surface biosensors, and display libraries. Expanding the applications of designed OMPs requires the identification of elements essential for β-barrel scaffold formation and stability. Here, we have designed chimeric 8-stranded OMPs composed of strand hybrids of Escherichia coli OmpX and Yersinia pestis Ail, and identified molecular motifs essential for β-barrel scaffold formation. For the OmpX/Ail chimeras, we find that the central hairpin strands β4-β5 in tandem are vital for β-barrel folding. We also show that the central hairpin can facilitate OMP assembly even when present as the N- or C-terminal strands. Further, the C-terminal β-signal and strand length are important but neither sufficient nor mutually exclusive for β-barrel assembly. Our results point to a nonstochastic model for assembly of chimeric β-barrels in lipidic micelles. The assembly likely follows a predefined nucleation at the central hairpin only when presented in tandem, with some influence from its absolute position in the barrel. Our findings can lead to the design of engineered barrels that retain the OMP assembly elements necessary to attain well-folded, stable, yet malleable scaffolds, for bionanotechnology applications.
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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.