ArticleProceedings of the National Academy of Sciences of the United States of America2010
Characterization of the two-protein complex in Escherichia coli responsible for lipopolysaccharide assembly at the outer membrane.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.
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Who cites it
139 citing papers in PubMed, 211 citations in OpenAlex.
- Article
- Lipopolysaccharide insertion and vesicle mediated turnover drive growth independent outer membrane adaptation in Escherichia coli.Nature communications · 2026Article
- Marine Antimicrobial Peptide as a Promising Alternative to Polymyxin B.Marine drugs · 2026Article
- Lipopolysaccharide confinement in the bacterial outer membrane is governed by interactions within the conserved Lipid A anchor.The EMBO journal · 2026Article
- Structural snapshots of Pseudomonas aeruginosa LptBNature communications · 2025Article
- Article
- Coordinated Biosynthesis of Essential Cell Envelope Components: Lipopolysaccharide and Fatty Acids Requires LapD, Acyl Carrier Protein, and Fully Hexaacylated Lipid A.International journal of molecular sciences · 2025Article
- Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function.Nature communications · 2025Article
- Species-Specific Stress Responses to Selenium Nanoparticles inNanomaterials (Basel, Switzerland) · 2025Article
- Adaptive genetics reveals constraints on protein structure/function by evolving E. coli under constant nutrient limitation.BMC biology · 2025Article
- Inhibiting Lipopolysaccharide Biogenesis: The More You Know the Further You Go.Annual review of biochemistry · 2025Review
- Surface lipoprotein sorting by crosstalk between Lpt and Lol pathways in gram-negative bacteria.Nature communications · 2025Article
- Outer membrane lipoproteins: late to the party, but the center of attention.Journal of bacteriology · 2025Review
- Recent advances in understanding of enterobacterial common antigen synthesis and regulation.Open biology · 2025Review
- Comprehensive In Vitro Evaluation of Antibacterial, Antioxidant, and Computational Insights intoPlants (Basel, Switzerland) · 2024Article
- Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Determination of Initial Rates of Lipopolysaccharide Transport.Biochemistry · 2024Article
- Effects of pleiotropicJournal of bacteriology · 2024Article
- Structural Insights into the Lipopolysaccharide Transport (Lpt) System as a Novel Antibiotic Target.Journal of microbiology (Seoul, Korea) · 2024Review
- Conformational investigation of the asymmetric periplasmic domains ofApplied magnetic resonance · 2024Article
79 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Lipopolysaccharide (LPS) is the major glycolipid that is present in the outer membranes (OMs) of most Gram-negative bacteria. LPS molecules are assembled with divalent metal cations in the outer leaflet of the OM to form an impervious layer that prevents toxic compounds from entering the cell. For most Gram-negative bacteria, LPS is essential for growth. In Escherichia coli, eight essential proteins have been identified to function in the proper assembly of LPS following its biosynthesis. This assembly process involves release of LPS from the inner membrane (IM), transport across the periplasm, and insertion into the outer leaflet of the OM. Here, we describe the biochemical characterization of the two-protein complex consisting of LptD and LptE that is responsible for the assembly of LPS at the cell surface. We can overexpress and purify LptD and LptE as a stable complex in a 1:1 stoichiometry. LptD contains a soluble N-terminal domain and a C-terminal transmembrane domain. LptE stabilizes LptD by interacting strongly with the C-terminal domain of LptD. We also demonstrate that LptE binds LPS specifically and may serve as a substrate recognition site at the OM.
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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.