2017
DOI: 10.1038/nsmb.3399
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Structural basis for lipopolysaccharide extraction by ABC transporter LptB2FG

Abstract: After biosynthesis, bacterial lipopolysaccharides (LPS) are transiently anchored to the outer leaflet of the inner membrane (IM). The ATP-binding cassette (ABC) transporter LptBFG extracts LPS molecules from the IM and transports them to the outer membrane. Here we report the crystal structure of nucleotide-free LptBFG from Pseudomonas aeruginosa. The structure reveals that lipopolysaccharide transport proteins LptF and LptG each contain a transmembrane domain (TMD), a periplasmic β-jellyroll-like domain and a… Show more

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Cited by 96 publications
(124 citation statements)
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References 52 publications
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“…The NBDs have moved in a “scissors‐like” motion similar to the transition between inward and outward‐open MsbA. A small degree of disengagement between the NBDs has also been reported for the heterodimeric ABC exporter TM287/288 (Hohl et al , 2012; Hohl et al , 2014), ABCG5/8 (Lee et al , 2016) and LptB 2 FG (Luo et al , 2017). …”
Section: Resultsmentioning
confidence: 78%
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“…The NBDs have moved in a “scissors‐like” motion similar to the transition between inward and outward‐open MsbA. A small degree of disengagement between the NBDs has also been reported for the heterodimeric ABC exporter TM287/288 (Hohl et al , 2012; Hohl et al , 2014), ABCG5/8 (Lee et al , 2016) and LptB 2 FG (Luo et al , 2017). …”
Section: Resultsmentioning
confidence: 78%
“…The McjD‐apo structure can be superimposed with the McjD‐AMPPNP structure with an rmsd of 2.1 Å over 569 Cα atoms; their TMDs can be superimposed with an rmsd of 0.7 Å over 290 Cα atoms. The heterodimeric human sterol apo‐ABCG5/8 (Lee et al , 2016) and Pseudomonas aeruginosa lipopolysaccharide apo‐LptB 2 FG (Luo et al , 2017) do not display intertwining either.…”
Section: Resultsmentioning
confidence: 99%
“…This observation is reminiscent of the distinct roles played by the TMDs of the Lol system for lipoprotein trafficking at the OM in E. coli (61). Such biochemical and genetic studies were nicely complemented by the resolution of the crystal structure of the LptB 2 FG complex from Pseudomonas aeruginosa in the nucleotide-free state (58). Notably, the arrangement of the TMDs of LptF and LptG defines a cavity whose surface is mainly hydrophobic, with the exception of the IM-periplasm interface, which is positively charged.…”
Section: Lps Detachment From the Immentioning
confidence: 79%
“…This cavity appears to be large enough to accommodate LPS, which, anchored at the IM outer leaflet, could enter via the lateral gates formed by the TMDs of LptF and LptG ( Fig. 2A) (58). The P. aeruginosa LptB 2 FG structure is thought to represent the resting state of the transporter, with the lateral gates that could further open upon ATP hydrolysis to allow LPS loading into the LPS-binding cavity.…”
Section: Lps Detachment From the Immentioning
confidence: 99%
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