ArticleStructure (London, England : 1993)2010
PagP crystallized from SDS/cosolvent reveals the route for phospholipid access to the hydrocarbon ruler.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Nature communications · 2026Article
- Membrane Protein Engineering with Rosetta.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Hydrophobic Characteristic Is Energetically Preferred for Cysteine in a Model Membrane Protein.Biophysical journal · 2019Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Comparison of NMR and crystal structures of membrane proteins and computational refinement to improve model quality.Proteins · 2018Article
- Outer membrane protein folding from an energy landscape perspective.BMC biology · 2017Review
- Structural basis for catalysis at the membrane-water interface.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Influence of Protein Scaffold on Side-Chain Transfer Free Energies.Biophysical journal · 2017Article
- Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.The Journal of biological chemistry · 2017Article
- Identification of a Large Family of Slam-Dependent Surface Lipoproteins in Gram-Negative Bacteria.Frontiers in cellular and infection microbiology · 2017Article
- 2-Methyl-2,4-pentanediol (MPD) boosts as detergent-substitute the performance of ß-barrel hybrid catalyst for phenylacetylene polymerization.Beilstein journal of organic chemistry · 2017Article
- Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability.Biochemistry · 2016Article
- Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.Structure (London, England : 1993) · 2016Article
- Large-scale identification of membrane proteins with properties favorable for crystallization.Protein science : a publication of the Protein Society · 2015Article
- Lipopolysaccharide transport to the cell surface: periplasmic transport and assembly into the outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
- Crystal structure of a COG4313 outer membrane channel.Scientific reports · 2015Article
- Amphipols outperform dodecylmaltoside micelles in stabilizing membrane protein structure in the gas phase.Analytical chemistry · 2015Article
- Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?Archives of biochemistry and biophysics · 2014Review
- Article
- PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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8 authors.
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Abstract
Enzymatic reactions involving bilayer lipids occur in an environment with strict physical and topological constraints. The integral membrane enzyme PagP transfers a palmitoyl group from a phospholipid to lipid A in order to assist Escherichia coli in evading host immune defenses during infection. PagP measures the palmitoyl group with an internal hydrocarbon ruler that is formed in the interior of the eight-stranded antiparallel β barrel. The access and egress of the palmitoyl group is thought to take a lateral route from the bilayer phase to the barrel interior. Molecular dynamics, mutagenesis, and a 1.4 A crystal structure of PagP in an SDS / 2-methyl-2,4-pentanediol (MPD) cosolvent system reveal that phospholipid access occurs at the crenel present between strands F and G of PagP. In this way, the phospholipid head group can remain exposed to the cell exterior while the lipid acyl chain remains in a predominantly hydrophobic environment as it translocates to the protein interior.
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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.