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TitleMolecular mechanism of phospholipid transport at the bacterial outer membrane interface.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 8285, Year 2023
Publish dateDec 13, 2023
AuthorsJiang Yeow / Min Luo / Shu-Sin Chng /
PubMed AbstractThe outer membrane (OM) of Gram-negative bacteria is an asymmetric lipid bilayer with outer leaflet lipopolysaccharides and inner leaflet phospholipids (PLs). This unique lipid asymmetry renders the ...The outer membrane (OM) of Gram-negative bacteria is an asymmetric lipid bilayer with outer leaflet lipopolysaccharides and inner leaflet phospholipids (PLs). This unique lipid asymmetry renders the OM impermeable to external insults, including antibiotics and bile salts. To maintain this barrier, the OmpC-Mla system removes mislocalized PLs from the OM outer leaflet, and transports them to the inner membrane (IM); in the first step, the OmpC-MlaA complex transfers PLs to the periplasmic chaperone MlaC, but mechanistic details are lacking. Here, we biochemically and structurally characterize the MlaA-MlaC transient complex. We map the interaction surfaces between MlaA and MlaC in Escherichia coli, and show that electrostatic interactions are important for MlaC recruitment to the OM. We further demonstrate that interactions with MlaC modulate conformational states in MlaA. Finally, we solve a 2.9-Å cryo-EM structure of a disulfide-trapped OmpC-MlaA-MlaC complex in nanodiscs, reinforcing the mechanism of MlaC recruitment, and highlighting membrane thinning as a plausible strategy for directing lipids for transport. Our work offers critical insights into retrograde PL transport by the OmpC-Mla system in maintaining OM lipid asymmetry.
External linksNat Commun / PubMed:38092770 / PubMed Central
MethodsEM (single particle)
Resolution2.93 - 3.42 Å
Structure data

35250

8i8r

EMDB-35250, PDB-8i8r:
Cryo-EM Structure of OmpC3-MlaA Complex in MSP2N2 Nanodiscs
Method: EM (single particle) / Resolution: 2.93 Å

EMDB-35251: Density map of the OmpC3-MlaA3 complex in MSP2N2 nanodiscs disulfide-bonded to MlaC
Method: EM (single particle) / Resolution: 3.42 Å

EMDB-35252: Density map of the OmpC3-MlaA2 complex in MSP2N2 nanodiscs disulfide-bonded to MlaC
Method: EM (single particle) / Resolution: 3.19 Å

35253

8i8x

EMDB-35253, PDB-8i8x:
Cryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs
Method: EM (single particle) / Resolution: 3.25 Å

Chemicals

ChemComp-KDL:
(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]-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]-5-oxidanyl-oxan-4-yl]oxy-4,5-bis(oxidanyl)oxane-2-carboxylic acid

Source
  • Escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsLIPID TRANSPORT / bacteria / outer membrane / phospholipid / lipid asymmetry / membrane protein / protein complex structure / channel

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