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@ARTICLE{Mann:894345,
      author       = {Mann, Daniel and Fan, Junping and Somboon, Kamolrat and
                      Farrell, Daniel P. and Muenks, Andrew and Tzokov, Svetomir
                      B. and DiMaio, Frank and Khalid, Syma and Miller, Samuel I.
                      and Bergeron, Julien R. C.},
      title        = {{S}tructure and lipid dynamics in the maintenance of lipid
                      asymmetry inner membrane complex of {A}. baumannii},
      journal      = {Communications biology},
      volume       = {4},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2021-03191},
      pages        = {817},
      year         = {2021},
      abstract     = {Multi-resistant bacteria are a major threat in modern
                      medicine. The gram-negative coccobacillus Acinetobacter
                      baumannii currently leads the WHO list of pathogens in
                      critical need for new therapeutic development. The
                      maintenance of lipid asymmetry (MLA) protein complex is one
                      of the core machineries that transport lipids from/to the
                      outer membrane in gram-negative bacteria. It also
                      contributes to broad-range antibiotic resistance in several
                      pathogens, most prominently in A. baumannii. Nonetheless,
                      the molecular details of its role in lipid transport has
                      remained largely elusive. Here, we report the cryo-EM maps
                      of the core MLA complex, MlaBDEF, from the pathogen A.
                      baumannii, in the apo-, ATP- and ADP-bound states, revealing
                      multiple lipid binding sites in the cytosolic and
                      periplasmic side of the complex. Molecular dynamics
                      simulations suggest their potential trajectory across the
                      membrane. Collectively with the recently-reported structures
                      of the E. coli orthologue, this data also allows us to
                      propose a molecular mechanism of lipid transport by the MLA
                      system.},
      cin          = {ER-C-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 5352 - Understanding the Functionality of Soft
                      Matter and Biomolecular Systems (POF4-535)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-5352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34188171},
      UT           = {WOS:000671730300002},
      doi          = {10.1038/s42003-021-02318-4},
      url          = {https://juser.fz-juelich.de/record/894345},
}