期刊
CELL
卷 181, 期 3, 页码 653-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2020.03.030
关键词
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资金
- NIH/NIGMS [R00GM112982, R35GM128777]
- Damon Runyon Cancer Research Foundation [DFS-20-16]
- American Heart Association [20POST35210202]
- Summer Undergraduate Research Program at the NYU School of Medicine
- National Cancer Institute [ACB12002]
- National Institute of General Medical Sciences [AGM-12006]
- DOE Office of Science [DE-AC02-06CH11357]
- NIH-Office of Research Infrastructure Programs, High-End Instrumentation Grant [1S10OD012289-01A1]
- NYU Cancer Center Support Grant [NIH/NCI P30CA016087]
Gram-negative bacteria are surrounded by an outer membrane composed of phospholipids and lipopolysaccharide, which acts as a barrier and contributes to antibiotic resistance. The systems that mediate phospholipid trafficking across the periplasm, such as MCE (Mammalian Cell Entry) transporters, have not been well characterized. Our similar to 3.5 angstrom cryo-EM structure of the E. coli MCE protein LetB reveals an similar to 0.6 megadalton complex that consists of seven stacked rings, with a central hydrophobic tunnel sufficiently long to span the perk plasm. Lipids bind inside the tunnel, suggesting that it functions as a pathway for lipid transport. Cryo-EM structures in the open and closed states reveal a dynamic tunnel lining, with implications for gating or substrate translocation. Our results support a model in which LetB establishes a physical link between the two membranes and creates a hydrophobic pathway for the translocation of lipids across the periplasm.
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