{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Malojcic G"],"funding":["NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["9467-72"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4084488"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["111(26)"],"pubmed_abstract":["The assembly of lipopolysaccharide (LPS) on the surface of Gram-negative bacterial cells is essential for their viability and is achieved by the seven-protein LPS transport (Lpt) pathway. The outer membrane (OM) lipoprotein LptE and the β-barrel membrane protein LptD form a complex that assembles LPS into the outer leaflet of the OM. We report a crystal structure of the Escherichia coli OM lipoprotein LptE at 2.34 Å. The structure reveals homology to eukaryotic LPS-binding proteins and allowed for the prediction of an LPS-binding site, which was confirmed by genetic and biophysical experiments. Specific point mutations at this site lead to defects in OM biogenesis. We show that wild-type LptE disrupts LPS-LPS interactions in vitro and that these mutations decrease the ability of LptE to di"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface."],"pmcid":["PMC4084488"],"funding_grant_id":["R01 GM034821","P41 GM111244","R37 GM034821","AI081059","R01 AI081059","GM034821"],"pubmed_authors":["Silhavy TJ","Grabowicz M","Andres D","Kahne D","Malojcic G","Ruiz N","George AH"],"additional_accession":[]},"is_claimable":false,"name":"LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.","description":"The assembly of lipopolysaccharide (LPS) on the surface of Gram-negative bacterial cells is essential for their viability and is achieved by the seven-protein LPS transport (Lpt) pathway. The outer membrane (OM) lipoprotein LptE and the β-barrel membrane protein LptD form a complex that assembles LPS into the outer leaflet of the OM. We report a crystal structure of the Escherichia coli OM lipoprotein LptE at 2.34 Å. The structure reveals homology to eukaryotic LPS-binding proteins and allowed for the prediction of an LPS-binding site, which was confirmed by genetic and biophysical experiments. Specific point mutations at this site lead to defects in OM biogenesis. We show that wild-type LptE disrupts LPS-LPS interactions in vitro and that these mutations decrease the ability of LptE to di","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 Jul","modification":"2026-05-03T15:30:13.822Z","creation":"2019-03-27T01:31:32Z"},"accession":"S-EPMC4084488","cross_references":{"pubmed":["24938785"],"doi":["10.1073/pnas.1402746111"]}}