ArticleMolecular biotechnology2011
The use of the condensed single protein production system for isotope-labeled outer membrane proteins, OmpA and OmpX in E. coli.
Article in Molecular biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Article
- 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
- Advances in NMR structures of integral membrane proteins.Current opinion in structural biology · 2013Review
- In situ structural characterization of a recombinant protein in native Escherichia coli membranes with solid-state magic-angle-spinning NMR.Journal of the American Chemical Society · 2011Article
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4 authors.
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Abstract
Gram-negative bacteria consist of two independent membranes, the inner cytoplasmic membrane and the outer membrane. The outer membrane contains a number of β-barrel proteins such as OmpF, OmpC, OmpA, and OmpX. In this article, we explored to use the condensed Single Protein Production (cSPP) system for isotope labelling of OmpA and OmpX for NMR structural study, both of which are known to consist of eight β-strands forming a barrel in the outer membrane. Using a deletion strain lacking all major outer membrane proteins, both OmpA and OmpX were expressed well in a 20-fold cSPP system. We demonstrated that outer membrane fractions prepared from the cSPP system in M9 medium containing ¹⁵N-NH₄Cl can be directly used for NMR structural study of the outer mebrane proteins without any further purification to get excellent [¹H-¹⁵N]-TROSY spectra. This method would be quite valuable for the study of pure proteins in their native membrane environment without the need of purification and reconstitution.
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