ArticleBiophysical journal2016
Full-Length OmpA: Structure, Function, and Membrane Interactions Predicted by Molecular Dynamics Simulations.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 68 citations in OpenAlex.
- Article
- OmpA_C-Like Domain of PorE Is Essential for PorE Function in the Type IX Secretion System (T9SS) of Porphyromonas gingivalis and Some T9SS Cargo Proteins Are Secreted in a PorE-Independent Manner.Microbiology and immunology · 2026Article
- The Perspectives of Combining Antibiotics with Saponins-Herbal Excipients.Molecules (Basel, Switzerland) · 2025Review
- OmpA controls order in the outer membrane and shares the mechanical load.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Overexpression of outer membrane protein A (OmpA) increases aminoglycoside sensitivity in mycobacteria.BMC microbiology · 2024Article
- Molecular Crowding Alters the Interactions of Polymyxin Lipopeptides within the Periplasm ofThe journal of physical chemistry. B · 2024Article
- Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.International journal of molecular sciences · 2023Review
- Article
- NlpE Is an OmpA-Associated Outer Membrane Sensor of the Cpx Envelope Stress Response.Journal of bacteriology · 2023Article
- Non-typeableFrontiers in cellular and infection microbiology · 2023Article
- In-Cell Labeling and Mass Spectrometry for Systems-Level Structural Biology.Chemical reviews · 2022Review
- What have molecular simulations contributed to understanding of Gram-negative bacterial cell envelopes?Microbiology (Reading, England) · 2022Review
- Article
- Article
- A Polyclonal Antibody Raised against theBiomedicines · 2021Article
- Phase separation in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- New Provisional Function of OmpA frommSystems · 2021Article
- Dinoroseobacter shibae Outer Membrane Vesicles Are Enriched for the Chromosome Dimer Resolution SitemSystems · 2021Article
- Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
OmpA is a multidomain protein found in the outer membranes of most Gram-negative bacteria. Despite a wealth of reported structural and biophysical studies, the structure-function relationships of this protein remain unclear. For example, it is still debated whether it functions as a pore, and the precise molecular role it plays in attachment to the peptidoglycan of the periplasm is unknown. The absence of a consensus view is partly due to the lack of a complete structure of the full-length protein. To address this issue, we performed molecular-dynamics simulations of the full-length model of the OmpA dimer proposed by Robinson and co-workers. The N-terminal domains were embedded in an asymmetric model of the outer membrane, with lipopolysaccharide molecules in the outer leaflet and phospholipids in the inner leaflet. Our results reveal a large dimerization interface within the membrane environment, ensuring that the dimer is stable over the course of the simulations. The linker is flexible, expanding and contracting to pull the globular C-terminal domain up toward the membrane or push it down toward the periplasm, suggesting a possible mechanism for providing mechanical stability to the cell. The external loops were more stabilized than was observed in previous studies due to the extensive dimerization interface and presence of lipopolysaccharide molecules in our outer-membrane model, which may have functional consequences in terms of OmpA adhesion to host cells. In addition, the pore-gating behavior of the protein was modulated compared with previous observations, suggesting a possible role for dimerization in channel regulation.
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