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TitleStructure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii.
Journal, issue, pagesCommun Biol, Vol. 4, Issue 1, Page 817, Year 2021
Publish dateJun 29, 2021
AuthorsDaniel Mann / Junping Fan / Kamolrat Somboon / Daniel P Farrell / Andrew Muenks / Svetomir B Tzokov / Frank DiMaio / Syma Khalid / Samuel I Miller / Julien R C Bergeron /
PubMed AbstractMulti-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 ...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.
External linksCommun Biol / PubMed:34188171 / PubMed Central
MethodsEM (single particle)
Resolution3.9 - 4.43 Å
Structure data

11082

6z5u

EMDB-11082, PDB-6z5u:
Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-11083:
Cryo-EM structure of the Acinetobacter baumannii MlaBDEF complex
Method: EM (single particle) / Resolution: 4.24 Å

EMDB-11084:
Cryo-EM structure of the Acinetobacter baumannii MlaBDEF complex bound to ADP
Method: EM (single particle) / Resolution: 4.43 Å

EMDB-14398: Cryo-EM structure of the A. baumannii MlaBDEF complex bound to APPNHP
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • acinetobacter baumannii (bacteria)
KeywordsMEMBRANE PROTEIN / lipid transport / antibiotic resistance / ABC transporter

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