期刊
PLOS BIOLOGY
卷 20, 期 10, 页码 -出版社
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pbio.3001823
关键词
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资金
- National Natural Science Foundation of China [31625009, 21575065]
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDB37020201]
- Ministry of Science and Technology [2016YFA0500404]
- China Postdoctoral Science Foundation [BX20190356]
This study reports the structures of LolCDE in different states and provides insights into the molecular details of the lipoprotein sorting mechanism mediated by LolCDE.
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 angstrom. 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.
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