ArticleJournal of molecular biology2012
Engineered oligomerization state of OmpF protein through computational design decouples oligomer dissociation from unfolding.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Permeabilisation of the Outer Membrane of Escherichia coli for Enhanced Transport of Complex Molecules.Microbial biotechnology · 2025Article
- Dawn of a New Era for Membrane Protein Design.Biodesign research · 2022Review
- Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes.mBio · 2021Article
- The architecture of the OmpC-MlaA complex sheds light on the maintenance of outer membrane lipid asymmetry inThe Journal of biological chemistry · 2018Article
- High-resolution structure prediction ofProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Probing the binding affinities of imipenem and ertapenem for outer membrane carboxylate channel D1 (OccD1) from P. aeruginosa: simulation studies.Journal of molecular modeling · 2017Article
- Outer membrane protein design.Current opinion in structural biology · 2017Review
- In Silico Structure and Sequence Analysis of Bacterial Porins and Specific Diffusion Channels for Hydrophilic Molecules: Conservation, Multimericity and Multifunctionality.International journal of molecular sciences · 2016Article
- Outer Membrane Protein Folding and Topology from a Computational Transfer Free Energy Scale.Journal of the American Chemical Society · 2016Article
- Computational redesign of the lipid-facing surface of the outer membrane protein OmpA.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Weakly stable regions and protein-protein interactions in beta-barrel membrane proteins.Current pharmaceutical design · 2014Review
- A 3-dimensional trimeric β-barrel model for Chlamydia MOMP contains conserved and novel elements of Gram-negative bacterial porins.PloS one · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Biogenesis of β-barrel membrane proteins is a complex, multistep, and as yet incompletely characterized process. The bacterial porin family is perhaps the best-studied protein family among β-barrel membrane proteins that allows diffusion of small solutes across the bacterial outer membrane. In this study, we have identified residues that contribute significantly to the protein-protein interaction (PPI) interface between the chains of outer membrane protein F (OmpF), a trimeric porin, using an empirical energy function in conjunction with an evolutionary analysis. By replacing these residues through site-directed mutagenesis either with energetically favorable residues or substitutions that do not occur in natural bacterial outer membrane proteins, we succeeded in engineering OmpF mutants with dimeric and monomeric oligomerization states instead of a trimeric oligomerization state. Moreover, our results suggest that the oligomerization of OmpF proceeds through a series of interactions involving two distinct regions of the extensive PPI interface: two monomers interact to form a dimer through the PPI interface near G19. This dimer then interacts with another monomer through the PPI interface near G135 to form a trimer. We have found that perturbing the PPI interface near G19 results in the formation of the monomeric OmpF only. Thermal denaturation of the designed dimeric OmpF mutant suggests that oligomer dissociation can be separated from the process of protein unfolding. Furthermore, the conserved site near G57 and G59 is important for the PPI interface and might provide the essential scaffold for PPIs.
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Registered trials
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