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Structure paper

TitleStructural basis of lipopolysaccharide extraction by the LptBFGC complex.
Journal, issue, pagesNature, Vol. 567, Issue 7749, Page 486-490, Year 2019
Publish dateMar 20, 2019
AuthorsYanyan Li / Benjamin J Orlando / Maofu Liao /
PubMed AbstractIn Gram-negative bacteria, lipopolysaccharide is essential for outer membrane formation and antibiotic resistance. The seven lipopolysaccharide transport (Lpt) proteins A-G move lipopolysaccharide ...In Gram-negative bacteria, lipopolysaccharide is essential for outer membrane formation and antibiotic resistance. The seven lipopolysaccharide transport (Lpt) proteins A-G move lipopolysaccharide from the inner to the outer membrane. The ATP-binding cassette transporter LptBFG, which tightly associates with LptC, extracts lipopolysaccharide out of the inner membrane. The mechanism of the LptBFG-LptC complex (LptBFGC) and the role of LptC in lipopolysaccharide transport are poorly understood. Here we characterize the structures of LptBFG and LptBFGC in nucleotide-free and vanadate-trapped states, using single-particle cryo-electron microscopy. These structures resolve the bound lipopolysaccharide, reveal transporter-lipopolysaccharide interactions with side-chain details and uncover how the capture and extrusion of lipopolysaccharide are coupled to conformational rearrangements of LptBFGC. LptC inserts its transmembrane helix between the two transmembrane domains of LptBFG, which represents a previously unknown regulatory mechanism for ATP-binding cassette transporters. Our results suggest a role for LptC in achieving efficient lipopolysaccharide transport, by coordinating the action of LptBFG in the inner membrane and Lpt protein interactions in the periplasm.
External linksNature / PubMed:30894744 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 5.9 Å
Structure data

9118

6mhu

EMDB-9118, PDB-6mhu:
Nucleotide-free Cryo-EM Structure of E.coli LptB2FG Transporter
Method: EM (single particle) / Resolution: 4.0 Å

9124

6mhz

EMDB-9124, PDB-6mhz:
Vanadate trapped Cryo-EM Structure of E.coli LptB2FG Transporter
Method: EM (single particle) / Resolution: 4.1 Å

9125

6mi7

EMDB-9125, PDB-6mi7:
Nucleotide-free Cryo-EM Structure of E.coli LptB2FGC
Method: EM (single particle) / Resolution: 4.2 Å

9126

6mi8

EMDB-9126, PDB-6mi8:
Cryo-EM Structure of vanadate-trapped E.coli LptB2FGC
Method: EM (single particle) / Resolution: 4.3 Å

EMDB-9128:
Cryo-EM Structure of E.coli LptB2FGC with LPS
Method: EM (single particle) / Resolution: 4.4 Å

EMDB-9129:
Cryo-EM Structure of E.coli LptB2FGC with long BJR
Method: EM (single particle) / Resolution: 4.8 Å

EMDB-9130:
Cryo-EM Structure of E.coli LptB2FGC with short BJR
Method: EM (single particle) / Resolution: 5.9 Å

Chemicals

ChemComp-JSG:
(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-2-[(2~{R},4~{R},5~{R},6~{R})-6-[(1~{R})-1,2-bis(oxidanyl)ethyl]-5-[(2~{S},3~{S},4~{R},5~{R},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-4-[(2~{R},3~{S},4~{R},5~{S},6~{R})-6-[(1~{S})-2-[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-[(1~{S})-1,2-bis(oxidanyl)ethyl]-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-1-oxidanyl-ethyl]-3,4-bis(oxidanyl)-5-phosphonooxy-oxan-2-yl]oxy-3-oxidanyl-5-phosphonooxy-oxan-2-yl]oxy-2-carboxy-2-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-5-[[(3~{R})-3-dodecanoyloxytetradecanoyl]amino]-6-[[(2~{R},3~{S},4~{R},5~{R},6~{R})-3-oxidanyl-5-[[(3~{R})-3-oxidanyltetradecanoyl]amino]-4-[(3~{R})-3-oxidanyltetradecanoyl]oxy-6-phosphonooxy-oxan-2-yl]methoxy]-3-phosphonooxy-4-[(3~{R})-3-tetradecanoyloxytetradecanoyl]oxy-oxan-2-yl]methoxy]oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid

ChemComp-AOV:
ADP ORTHOVANADATE / energy-carrying molecule analogue*YM

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM / Phosphatidylglycerol

Source
  • escherichia coli (strain k12) (bacteria)
  • Escherichia coli (E. coli)
KeywordsTRANSPORT PROTEIN/Hydrolase / ABC transporter / lipopolysaccharide / LPS / nanodisc / TRANSPORT PROTEIN-Hydrolase complex / HYDROLASE/TRANSPORT PROTEIN / MEMBRANE PROTEIN / HYDROLASE-TRANSPORT PROTEIN complex

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