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-Structure paper
Title | Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli. |
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Journal, issue, pages | PLoS Biol, Vol. 20, Issue 10, Page e3001823, Year 2022 |
Publish date | Oct 13, 2022 |
Authors | Weiwei Bei / Qingshan Luo / Huigang Shi / Haizhen Zhou / Min Zhou / Xinzheng Zhang / Yihua Huang / |
PubMed Abstract | Bacterial lipoproteins perform a diverse array of functions including bacterial envelope biogenesis and microbe-host interactions. Lipoproteins in gram-negative bacteria are sorted to the outer ...Bacterial lipoproteins perform a diverse array of functions including bacterial envelope biogenesis and microbe-host interactions. Lipoproteins in gram-negative bacteria are sorted to the outer membrane (OM) via the localization of lipoproteins (Lol) export pathway. The ATP-binding cassette (ABC) transporter LolCDE initiates the Lol pathway by selectively extracting and transporting lipoproteins for trafficking. Here, we report cryo-EM structures of LolCDE in apo, lipoprotein-bound, and AMPPNP-bound states at a resolution of 3.5 to 4.2 Å. Structure-based disulfide crosslinking, photo-crosslinking, and functional complementation assay verify the apo-state structure and reveal the molecular details regarding substrate selectivity and substrate entry route. Our studies snapshot 3 functional states of LolCDE in a transport cycle, providing deep insights into the mechanisms that underlie LolCDE-mediated lipoprotein sorting in E. coli. |
External links | PLoS Biol / PubMed:36228045 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 - 4.2 Å |
Structure data | EMDB-31802, PDB-7v8i: EMDB-31803, PDB-7v8l: EMDB-31804, PDB-7v8m: |
Chemicals | ChemComp-MG: ChemComp-ANP: ChemComp-PCJ: |
Source |
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Keywords | MEMBRANE PROTEIN / ABC transporter / lipoprotein |