ArticleStructure (London, England : 1993)2014
Mass spectrometry defines the C-terminal dimerization domain and enables modeling of the structure of full-length OmpA.
Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 57 citations in OpenAlex.
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- Outer membrane protein A (OmpA) as a potential therapeutic target for Acinetobacter baumannii infection.Journal of biomedical science · 2020Review
- Interrogating Membrane Protein Structure and Lipid Interactions by Native Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The Mutation of Conservative Asp268 Residue in the Peptidoglycan-Associated Domain of the OmpA Protein Affects MultipleMolecules (Basel, Switzerland) · 2019Article
- Protein assemblies ejected directly from native membranes yield complexes for mass spectrometry.Science (New York, N.Y.) · 2018Article
- Outer Membrane Protein of Gut Commensal Microorganism Induces Autoantibody Production and Extra-Intestinal Gland Inflammation in Mice.International journal of molecular sciences · 2018Article
- Braun's Lipoprotein Facilitates OmpA Interaction with the Escherichia coli Cell Wall.Biophysical journal · 2017Article
- Insights into PG-binding, conformational change, and dimerization of the OmpA C-terminal domains from Salmonella enterica serovar Typhimurium and Borrelia burgdorferi.Protein science : a publication of the Protein Society · 2017Article
- Integral membrane proteins: bottom-up, top-down and structural proteomics.Expert review of proteomics · 2017Review
- Allelic Variation in Outer Membrane Protein A and Its Influence on Attachment ofFrontiers in microbiology · 2017Article
- TheBiochemistry and biophysics reports · 2016Article
- In vivo protein interaction network analysis reveals porin-localized antibiotic inactivation in Acinetobacter baumannii strain AB5075.Nature communications · 2016Article
- Full-Length OmpA: Structure, Function, and Membrane Interactions Predicted by Molecular Dynamics Simulations.Biophysical journal · 2016Article
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7 authors at 2 institutions in 2 countries.
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Abstract
The transmembrane domain of the outer membrane protein A (OmpA) from Escherichia coli is an excellent model for structural and folding studies of β-barrel membrane proteins. However, full-length OmpA resists crystallographic efforts, and the link between its function and tertiary structure remains controversial. Here we use site-directed mutagenesis and mass spectrometry of different constructs of OmpA, released in the gas phase from detergent micelles, to define the minimal region encompassing the C-terminal dimer interface. Combining knowledge of the location of the dimeric interface with molecular modeling and ion mobility data allows us to propose a low-resolution model for the full-length OmpA dimer. Our model of the dimer is in remarkable agreement with experimental ion mobility data, with none of the unfolding or collapse observed for full-length monomeric OmpA, implying that dimer formation stabilizes the overall structure and prevents collapse of the flexible linker that connects the two domains.
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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.