The outer membrane (OM) of Gram-negative bacteria, which consists of lipopolysaccharides (LPS) in the outer leaflet and phospholipids (PLs) in the inner leaflet, plays a key role in antibiotic resistance and pathogen virulence. The maintenance of lipid asymmetry (Mla) pathway is known to be involved in PL transport and contributes to the lipid homeostasis of the OM, yet the underlying molecular mechanism and the directionality of PL transport in this pathway remain elusive. Here, you can see the cryo-EM structures of the ATP-binding cassette (ABC) transporter MlaFEBD from P. areuginosa. The structures show that the MlaFEBD complex contains a total of twelve protein molecules with a stoichiometry of MlaF 2 E 2 B 2 D 6 , and binds a plethora of PLs at different locations. In contrast to canonical ABC transporters, nucleotide binding fails to trigger significant conformational changes of both MlaFEBD and MlaFEB in the nucleotide-binding and transmembrane domains of the ABC transporter (PDB code: 7CHA)
#molecularart ... #immolecular ... #ABCtransporter ... #Pseudomonas ... #conformation ... #membrane ... #outermembrane ... #nucleotide ... Rendered with @proteinimaging and polished with @corelphotopaint
#molecularart ... #immolecular ... #ABCtransporter ... #Pseudomonas ... #conformation ... #membrane ... #outermembrane ... #nucleotide ... Rendered with @proteinimaging and polished with @corelphotopaint
