6Z5U
Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP
Summary for 6Z5U
| Entry DOI | 10.2210/pdb6z5u/pdb |
| EMDB information | 11082 |
| Descriptor | ABC transporter permease, Anti-sigma factor antagonist, MCE family protein, ... (6 entities in total) |
| Functional Keywords | lipid transport, antibiotic resistance, abc transporter, membrane protein |
| Biological source | Acinetobacter baumannii More |
| Total number of polymer chains | 12 |
| Total formula weight | 283002.86 |
| Authors | Mann, D.,Bergeron, J.R.C. (deposition date: 2020-05-27, release date: 2021-05-05, Last modification date: 2024-05-22) |
| Primary citation | Mann, D.,Fan, J.,Somboon, K.,Farrell, D.P.,Muenks, A.,Tzokov, S.B.,DiMaio, F.,Khalid, S.,Miller, S.I.,Bergeron, J.R.C. Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii. Commun Biol, 4:817-817, 2021 Cited by PubMed 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. PubMed: 34188171DOI: 10.1038/s42003-021-02318-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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