ArticleProceedings of the National Academy of Sciences of the United States of America2021
Gram-negative outer-membrane proteins with multiple β-barrel domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- metaRLK 2.0: An updated database of plant receptor-like kinases developed with structure- and deep learning-based functional annotation and classification.Plant communications · 2026Article
- Pathogen Evasion of Humoral Innate Immunity: Coping with C-Reactive Protein and Serum Amyloid A.International journal of molecular sciences · 2026Review
- Design of a Multi-Epitope Vaccine using β-barrel Outer Membrane Proteins Identified in Chlamydia trachomatis.The Journal of membrane biology · 2025Article
- Modulation of Root Hydrotropism and Recovery From Drought by MIZ1-like Genes in Tomato.Plant, cell & environment · 2025Article
- A computational model for lipid-anchored polysaccharide export by the outer membrane protein GfcD.Biophysical journal · 2024Article
- Characterization of Three New Outer Membrane Adhesion Proteins inMicroorganisms · 2023Article
- Specific, sensitive and quantitative protein detection by in-gel fluorescence.Nature communications · 2023Article
- Bacterial Outer Membrane Polysaccharide Export (OPX) Proteins Occupy Three Structural Classes with Selective β-Barrel Porin Requirements for Polymer Secretion.Microbiology spectrum · 2022Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Outer-membrane beta barrels (OMBBs) are found in the outer membrane of gram-negative bacteria and eukaryotic organelles. OMBBs fold as antiparallel β-sheets that close onto themselves, forming pores that traverse the membrane. Currently known structures include only one barrel, of 8 to 36 strands, per chain. The lack of multi-OMBB chains is surprising, as most OMBBs form oligomers, and some function only in this state. Using a combination of sensitive sequence comparison methods and coevolutionary analysis tools, we identify many proteins combining multiple beta barrels within a single chain; combinations that include eight-stranded barrels prevail. These multibarrels seem to be the result of independent, lineage-specific fusion and amplification events. The absence of multibarrels that are universally conserved in bacteria with an outer membrane, coupled with their frequent de novo genesis, suggests that their functions are not essential but rather beneficial in specific environments. Adjacent barrels of complementary function within the same chain may allow for functions beyond those of the individual barrels.
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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.