6IC4

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

Summary for 6IC4

• Entry DOI: 10.2210/pdb6ic4/pdb
• EMDB information: 0007
• Descriptor: Toluene tolerance efflux transporter (ABC superfamily, PerI-bind), ABC transporter permease, ABC transporter ATP-binding protein, ... (4 entities in total)
• Functional Keywords: membrane protein antibiotic resistance abc transporter, protein transport
• Biological source: Acinetobacter baumannii; More
• Total number of polymer chains: 12
• Total formula weight: 246316.62

Authors

Bergeron, J.R.,Kollman, J.M. (deposition date: 2018-12-02, release date: 2019-01-23, Last modification date: 2024-05-15)

Primary citation

Kamischke, C.,Fan, J.,Bergeron, J.,Kulasekara, H.D.,Dalebroux, Z.D.,Burrell, A.,Kollman, J.M.,Miller, S.I.
The Acinetobacter baumannii Mla system and glycerophospholipid transport to the outer membrane.
Elife, 8:-, 2019

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 transposon mutants and identified a number of mutants with OM defects, including an ABC transporter system homologous to the Mla system in 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 OM integrity and antibiotic sensitivity suggests that its components may serve as new antimicrobial therapeutic targets.

PubMed: 30638443
DOI: 10.7554/eLife.40171

Experimental method

ELECTRON MICROSCOPY (8.7 Å)