This title appears in the Scientific Report :
2021
Please use the identifier:
http://hdl.handle.net/2128/28654 in citations.
Please use the identifier: http://dx.doi.org/10.1038/s42003-021-02318-4 in citations.
Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii
Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii
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...
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Personal Name(s): | Mann, Daniel |
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Fan, Junping / Somboon, Kamolrat / Farrell, Daniel P. / Muenks, Andrew / Tzokov, Svetomir B. / DiMaio, Frank / Khalid, Syma / Miller, Samuel I. / Bergeron, Julien R. C. (Corresponding author) | |
Contributing Institute: |
Strukturbiologie; ER-C-3 |
Published in: | Communications biology, 4 (2021) 1, S. 817 |
Imprint: |
London
Springer Nature
2021
|
DOI: |
10.1038/s42003-021-02318-4 |
PubMed ID: |
34188171 |
Document Type: |
Journal Article |
Research Program: |
Understanding the Functionality of Soft Matter and Biomolecular Systems Molecular Information Processing in Cellular Systems |
Link: |
OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1038/s42003-021-02318-4 in citations.
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. |