期刊
STRUCTURE
卷 27, 期 7, 页码 1114-+出版社
CELL PRESS
DOI: 10.1016/j.str.2019.04.007
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资金
- US Department of Energy (DOE)
- DOE Office of Biological and Environmental Research
- National Institute of General Medical Sciences (NIGMS)
- NIH [R01 GM118594, R01 GM098538, R01-GM123455, U54-GM087519, P41-GM104601]
- NIH
MsbA is an essential ATP-binding cassette transporter in Gram-negative bacteria that transports lipid A and lipopolysaccharide from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. Here we report the X-ray structure of MsbA from Salmonella typhimurium at 2.8-angstrom resolution in an inward-facing conformation after cocrystallization with lipid A and using a stabilizing facial amphiphile. The structure displays a large amplitude opening in the transmembrane portal, which is likely required for lipid A to pass from its site of synthesis into the protein-enclosed transport pathway. Putative lipid A density is observed further inside the transmembrane cavity, consistent with a trap and flip model. Additional electron density attributed to lipid A is observed near an outer surface cleft at the periplasmic ends of the transmembrane helices. These findings provide new structural insights into the lipid A transport pathway through comparative analysis with existing MsbA structures.
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