{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Qiao W"],"funding":["National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["354"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11671585"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(1)"],"pubmed_abstract":["Outer membrane (OM) lipoproteins serve vital roles in Gram-negative bacteria, contributing to their pathogenicity and drug resistance. For these lipoproteins to function, they must be transported from the inner membrane (IM), where they are assembled, to the OM by the ABC transporter LolCDE. We have previously captured structural snapshots of LolCDE in multiple states, revealing its dynamic conformational changes. However, the exact mechanism by which LolCDE recognizes and transfers lipoprotein between domains remains unclear. Here, we characterized the E. coli LolCDE complex bound with endogenous lipoprotein or ATP to explore the molecular features governing its substrate binding and transport functions. We found that the N-terminal unstructured linker of lipoprotein is critical for effic"],"journal":["Signal transduction and targeted therapy"],"pubmed_title":["Deciphering the molecular basis of lipoprotein recognition and transport by LolCDE."],"pmcid":["PMC11671585"],"funding_grant_id":["32000844","82372297","31900039","81971974"],"pubmed_authors":["Ding BS","Yang L","Zhao C","Shen C","Chang S","Qiao W","Ying B","Luo Q","Lu G","Zhang Z","Dong H","Xiang Y","Chen Y","Pang J","Wang X","Tang X"],"additional_accession":[]},"is_claimable":false,"name":"Deciphering the molecular basis of lipoprotein recognition and transport by LolCDE.","description":"Outer membrane (OM) lipoproteins serve vital roles in Gram-negative bacteria, contributing to their pathogenicity and drug resistance. For these lipoproteins to function, they must be transported from the inner membrane (IM), where they are assembled, to the OM by the ABC transporter LolCDE. We have previously captured structural snapshots of LolCDE in multiple states, revealing its dynamic conformational changes. However, the exact mechanism by which LolCDE recognizes and transfers lipoprotein between domains remains unclear. Here, we characterized the E. coli LolCDE complex bound with endogenous lipoprotein or ATP to explore the molecular features governing its substrate binding and transport functions. We found that the N-terminal unstructured linker of lipoprotein is critical for effic","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-05-02T14:25:33.079Z","creation":"2025-04-21T16:34:59.52Z"},"accession":"S-EPMC11671585","cross_references":{"pubmed":["39725716"],"doi":["10.1038/s41392-024-02067-w"]}}