6IC4

Cryo-EM structure of the A. baumannii MLA complex at 8.7 A resolution


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.70 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane.

Kamischke, C.Fan, J.Bergeron, J.Kulasekara, H.D.Dalebroux, Z.D.Burrell, A.Kollman, J.M.Miller, S.I.

(2019) Elife 8

  • DOI: https://doi.org/10.7554/eLife.40171
  • Primary Citation of Related Structures:  
    6IC4

  • PubMed Abstract: 

    The outer membrane (OM) of Gram-negative bacteria serves as a selective permeability barrier that allows entry of essential nutrients while excluding toxic compounds, including antibiotics. The OM is asymmetric and contains an outer leaflet of lipopolysaccharides (LPS) or lipooligosaccharides (LOS) and an inner leaflet of glycerophospholipids (GPL). We screened Acinetobacter baumannii transposon mutants and identified a number of mutants with OM defects, including an ABC transporter system homologous to the Mla system in E. coli. We further show that this opportunistic, antibiotic-resistant pathogen uses this multicomponent protein complex and ATP hydrolysis at the inner membrane to promote GPL export to the OM. The broad conservation of the Mla system in Gram-negative bacteria suggests the system may play a conserved role in OM biogenesis. The importance of the Mla system to Acinetobacter baumannii OM integrity and antibiotic sensitivity suggests that its components may serve as new antimicrobial therapeutic targets.


  • Organizational Affiliation

    Department of Microbiology, University of Washington, Seattle, United States.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Toluene tolerance efflux transporter (ABC superfamily, PerI-bind)
A, B, C, D, E
A, B, C, D, E, F
183Acinetobacter baumanniiMutation(s): 0 
Gene Names: ttg2CSAMEA104305283_00402
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ABC transporter permease
G, H
257Acinetobacter baumanniiMutation(s): 0 
Gene Names: 
Membrane Entity: Yes 
UniProt
Find proteins for V5V9F4 (Acinetobacter baumannii)
Explore V5V9F4 
Go to UniProtKB:  V5V9F4
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UniProt GroupV5V9F4
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ABC transporter ATP-binding protein
I, J
233Acinetobacter baumanniiMutation(s): 0 
Gene Names: 
UniProt
Find proteins for A0A086HZU3 (Acinetobacter baumannii)
Explore A0A086HZU3 
Go to UniProtKB:  A0A086HZU3
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UniProt GroupA0A086HZU3
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Ttg2E
K, L
93Acinetobacter baumanniiMutation(s): 0 
Gene Names: SAMEA104305318_02185
UniProt
Find proteins for A0A333U4T6 (Acinetobacter baumannii)
Explore A0A333U4T6 
Go to UniProtKB:  A0A333U4T6
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UniProt GroupA0A333U4T6
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 8.70 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2019-01-23
    Type: Initial release
  • Version 1.1: 2020-09-30
    Changes: Database references