{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["13(1)"],"submitter":["Botte M"],"pubmed_abstract":["Lipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 Å resolution. In addition, a subset of particles allows to model a structure of a laterally fully op"],"journal":["Nature communications"],"pagination":["1826"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8983717"],"repository":["biostudies-literature"],"pubmed_title":["Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation."],"pmcid":["PMC8983717"],"pubmed_authors":["Chami M","Zimmermann I","Brunner JD","Cheng RKY","Seeger MA","Stahlberg H","Bocquet N","Bucher D","Hennig M","Ni D","Botte M","Schenck S","Trabuco M","Egloff P"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structures of a LptDE transporter in complex with Pro-macrobodies offer insight into lipopolysaccharide translocation.","description":"Lipopolysaccharides are major constituents of the extracellular leaflet in the bacterial outer membrane and form an effective physical barrier for environmental threats and for antibiotics in Gram-negative bacteria. The last step of LPS insertion via the Lpt pathway is mediated by the LptD/E protein complex. Detailed insights into the architecture of LptDE transporter complexes have been derived from X-ray crystallography. However, no structure of a laterally open LptD transporter, a transient state that occurs during LPS release, is available to date. Here, we report a cryo-EM structure of a partially opened LptDE transporter in complex with rigid chaperones derived from nanobodies, at 3.4 Å resolution. In addition, a subset of particles allows to model a structure of a laterally fully op","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-30T14:35:45.083Z","creation":"2024-11-05T18:27:09.414Z"},"accession":"S-EPMC8983717","cross_references":{"pubmed":["35383177"],"doi":["10.1038/s41467-022-29459-2"]}}